Protein Structure, Secondary
Amino Acid Sequence
Deuterium Exchange Measurement
Molecular Sequence Data
Protein Structure, Tertiary
Optical Rotatory Dispersion
Magnetic Resonance Spectroscopy
Molecular Dynamics Simulation
Spectrum Analysis, Raman
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Quaternary
Spectroscopy, Fourier Transform Infrared
Amino Acid Substitution
Hydrophobic and Hydrophilic Interactions
Fluorescence Resonance Energy Transfer
Electrophoresis, Polyacrylamide Gel
Spectrometry, Mass, Electrospray Ionization
Polymorphism, Single-Stranded Conformational
Electron Spin Resonance Spectroscopy
Microscopy, Atomic Force
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Cytochrome c Group
Recombinant Fusion Proteins
Protein Processing, Post-Translational
Serum Albumin, Bovine
Saccharomyces cerevisiae Proteins
Scattering, Small Angle
Amino Acid Motifs
Structural Homology, Protein
Nucleic Acid Denaturation
Protein Interaction Domains and Motifs
Polymerase Chain Reaction
Endocytosis: EH domains lend a hand. (1/52898)A number of proteins that have been implicated in endocytosis feature a conserved protein-interaction module known as an EH domain. The three-dimensional structure of an EH domain has recently been solved, and is likely to presage significant advances in understanding molecular mechanisms of endocytosis. (+info)
Membrane fusion: structure snared at last. (2/52898)The structure of the core of the neuronal 'SNARE complex', involved in neurotransmitter release, has been determined recently. Its topological similarity to viral fusion proteins suggests how the SNARE complex might facilitate membrane fusion. (+info)
Four dimers of lambda repressor bound to two suitably spaced pairs of lambda operators form octamers and DNA loops over large distances. (3/52898)Transcription factors that are bound specifically to DNA often interact with each other over thousands of base pairs  . Large DNA loops resulting from such interactions have been observed in Escherichia coli with the transcription factors deoR  and NtrC , but such interactions are not, as yet, well understood. We propose that unique protein complexes, that are not present in solution, may form specifically on DNA. Their uniqueness would make it possible for them to interact tightly and specifically with each other. We used the repressor and operators of coliphage lambda to construct a model system in which to test our proposition. lambda repressor is a dimer at physiological concentrations, but forms tetramers and octamers at a hundredfold higher concentration. We predict that two lambda repressor dimers form a tetramer in vitro when bound to two lambda operators spaced 24 bp apart and that two such tetramers interact to form an octamer. We examined, in vitro, relaxed circular plasmid DNA in which such operator pairs were separated by 2,850 bp and 2,470 bp. Of these molecules, 29% formed loops as seen by electron microscopy (EM). The loop increased the tightness of binding of lambda repressor to lambda operator. Consequently, repression of the lambda PR promoter in vivo was increased fourfold by the presence of a second pair of lambda operators, separated by a distance of 3,600 bp. (+info)
Probing interactions between HIV-1 reverse transcriptase and its DNA substrate with backbone-modified nucleotides. (4/52898)BACKGROUND: To gain a molecular understanding of a biochemical process, the crystal structure of enzymes that catalyze the reactions involved is extremely helpful. Often the question arises whether conformations obtained in this way appropriately reflect the reactivity of enzymes, however. Rates that characterize transitions are therefore compulsory experiments for the elucidation of the reaction mechanism. Such experiments have been performed for the reverse transcriptase of the type 1 human immunodeficiency virus (HIV-1 RT). RESULTS: We have developed a methodology to monitor the interplay between HIV-1 RT and its DNA substrate. To probe the protein-DNA interactions, the sugar backbone of one nucleotide was modified by a substituent that influenced the efficiency of the chain elongation in a characteristic way. We found that strand elongation after incorporation of the modified nucleotide follows a discontinuous efficiency for the first four nucleotides. The reaction efficiencies could be correlated with the distance between the sugar substituent and the enzyme. The model was confirmed by kinetic experiments with HIV-1 RT mutants. CONCLUSIONS: Experiments with HIV-1 RT demonstrate that strand-elongation efficiency using a modified nucleotide correlates well with distances between the DNA substrate and the enzyme. The functional group at the modified nucleotides acts as an 'antenna' for steric interactions that changes the optimal transition state. Kinetic experiments in combination with backbone-modified nucleotides can therefore be used to gain structural information about reverse transcriptases and DNA polymerases. (+info)
A hyperstable collagen mimic. (5/52898)BACKGROUND: Collagen is the most abundant protein in animals. Each polypeptide chain of collagen is composed of repeats of the sequence: Gly-X-Y, where X and Y are often L-proline (Pro) and 4(R)-hydroxy-L-proline (Hyp) residues, respectively. These chains are wound into tight triple helices of great stability. The hydroxyl group of Hyp residues contributes much to this conformational stability. The existing paradigm is that this stability arises from interstrand hydrogen bonds mediated by bridging water molecules. This model was tested using chemical synthesis to replace Hyp residues with 4(R)-fluoro-L-proline (Flp) residues. The fluorine atom in Flp residues does not form hydrogen bonds but does elicit strong inductive effects. RESULTS: Replacing the Hyp residues in collagen with Flp residues greatly increases triple-helical stability. The free energy contributed by the fluorine atom in Flp residues is twice that of the hydroxyl group in Hyp residues. The stability of the Flp-containing triple helix far exceeds that of any untemplated collagen mimic of similar size. CONCLUSIONS: Bridging water molecules contribute little to collagen stability. Rather, collagen stability relies on previously unappreciated inductive effects. Collagen mimics containing fluorine or other appropriate electron-withdrawing substituents could be the basis of new biomaterials for restorative therapies. (+info)
How do peptide synthetases generate structural diversity? (6/52898)Many low-molecular-weight peptides of microbial origin are synthesized nonribosomally on large multifunctional proteins, termed peptide synthetases. These enzymes contain repeated building blocks in which several defined domains catalyze specific reactions of peptide synthesis. The order of these domains within the enzyme determines the sequence and structure of the peptide product. (+info)
Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. (7/52898)The lysosomal cysteine proteases cathepsins S and L play crucial roles in the degradation of the invariant chain during maturation of MHC class II molecules and antigen processing. The p41 form of the invariant chain includes a fragment which specifically inhibits cathepsin L but not S. The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L. The structure of the p41 fragment demonstrates a novel fold, consisting of two subdomains, each stabilized by disulfide bridges. The first subdomain is an alpha-helix-beta-strand arrangement, whereas the second subdomain has a predominantly beta-strand arrangement. The wedge shape and three-loop arrangement of the p41 fragment bound to the active site cleft of cathepsin L are reminiscent of the inhibitory edge of cystatins, thus demonstrating the first example of convergent evolution observed in cysteine protease inhibitors. However, the different fold of the p41 fragment results in additional contacts with the top of the R-domain of the enzymes, which defines the specificity-determining S2 and S1' substrate-binding sites. This enables inhibitors based on the thyroglobulin type-1 domain fold, in contrast to the rather non-selective cystatins, to exhibit specificity for their target enzymes. (+info)
Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D. (8/52898)The crystal structure of profactor D, determined at 2.1 A resolution with an Rfree and an R-factor of 25.1 and 20.4%, respectively, displays highly flexible or disordered conformation for five regions: N-22, 71-76, 143-152, 187-193 and 215-223. A comparison with the structure of its mature serine protease, complement factor D, revealed major conformational changes in the similar regions. Comparisons with the zymogen-active enzyme pairs of chymotrypsinogen, trypsinogen and prethrombin-2 showed a similar distribution of the flexible regions. However, profactor D is the most flexible of the four, and its mature enzyme displays inactive, self-inhibited active site conformation. Examination of the surface properties of the N-terminus-binding pocket indicates that Ile16 may play the initial positioning role for the N-terminus, and Leu17 probably also helps in inducing the required conformational changes. This process, perhaps shared by most chymotrypsinogen-like zymogens, is followed by a factor D-unique step, the re-orientation of an external Arg218 to an internal position for salt-bridging with Asp189, leading to the generation of the self-inhibited factor D. (+info)
Proteins are complex biomolecules made up of amino acids that play a crucial role in many biological processes in the human body. In the medical field, proteins are studied extensively as they are involved in a wide range of functions, including: 1. Enzymes: Proteins that catalyze chemical reactions in the body, such as digestion, metabolism, and energy production. 2. Hormones: Proteins that regulate various bodily functions, such as growth, development, and reproduction. 3. Antibodies: Proteins that help the immune system recognize and neutralize foreign substances, such as viruses and bacteria. 4. Transport proteins: Proteins that facilitate the movement of molecules across cell membranes, such as oxygen and nutrients. 5. Structural proteins: Proteins that provide support and shape to cells and tissues, such as collagen and elastin. Protein abnormalities can lead to various medical conditions, such as genetic disorders, autoimmune diseases, and cancer. Therefore, understanding the structure and function of proteins is essential for developing effective treatments and therapies for these conditions.
Silica gel is a desiccant, which is a substance that absorbs moisture from the air. It is commonly used in the medical field to remove moisture from medical equipment, such as syringes, vials, and other medical devices, to prevent the growth of bacteria and other microorganisms that thrive in moist environments. Silica gel is also used in the production of certain medications, such as insulin, to maintain the stability and potency of the medication. In addition, silica gel is sometimes used in wound dressings to absorb excess moisture and promote healing.
Myoglobin is a protein found in muscle tissue that plays a crucial role in oxygen storage and delivery. It is responsible for storing oxygen in muscle cells and releasing it when needed during periods of high physical activity. Myoglobin is also involved in the regulation of muscle metabolism and the removal of waste products from muscle cells. In the medical field, myoglobin levels are often measured in blood tests to diagnose and monitor various conditions, including muscle injuries, heart attacks, and kidney disease. High levels of myoglobin in the blood can indicate muscle damage or injury, while low levels may suggest a problem with muscle metabolism or oxygen delivery. Myoglobinuria, a condition characterized by the presence of myoglobin in the urine, can also be a sign of muscle injury or disease.
Tryptophan is an essential amino acid that is required for the production of proteins in the body. It is also a precursor to the neurotransmitter serotonin, which plays a role in regulating mood, appetite, and sleep. In the medical field, tryptophan is often used to treat conditions such as depression, anxiety, and insomnia. It is also used to help manage symptoms of premenstrual syndrome (PMS) and to improve athletic performance. Tryptophan supplements are available over-the-counter, but it is important to talk to a healthcare provider before taking them, as they can interact with certain medications and may have side effects.
Anilino naphthalenesulfonates are a class of organic compounds that are used in various medical applications. They are typically synthesized by the reaction of naphthalene-1-sulfonic acid with aniline or substituted anilines. These compounds have a planar aromatic structure and are often used as dyes, pigments, and surfactants. In the medical field, anilino naphthalenesulfonates are used as antimalarial agents. They are effective against Plasmodium falciparum, the parasite responsible for the most severe form of malaria. Some examples of anilino naphthalenesulfonates used in this context include chloroquine and hydroxychloroquine. Anilino naphthalenesulfonates are also used as antiviral agents. They have been shown to be effective against a variety of viruses, including influenza, herpes simplex virus, and human immunodeficiency virus (HIV). Some examples of anilino naphthalenesulfonates used in this context include amantadine and rimantadine. In addition to their antimalarial and antiviral properties, anilino naphthalenesulfonates have also been studied for their potential use in the treatment of other medical conditions, such as cancer and inflammatory diseases. However, more research is needed to fully understand their therapeutic potential and to develop safe and effective treatments based on these compounds.
Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.
In the medical field, peptides are short chains of amino acids that are linked together by peptide bonds. They are typically composed of 2-50 amino acids and can be found in a variety of biological molecules, including hormones, neurotransmitters, and enzymes. Peptides play important roles in many physiological processes, including growth and development, immune function, and metabolism. They can also be used as therapeutic agents to treat a variety of medical conditions, such as diabetes, cancer, and cardiovascular disease. In the pharmaceutical industry, peptides are often synthesized using chemical methods and are used as drugs or as components of drugs. They can be administered orally, intravenously, or topically, depending on the specific peptide and the condition being treated.
In the medical field, water is a vital substance that is essential for the proper functioning of the human body. It is a clear, odorless, tasteless liquid that makes up the majority of the body's fluids, including blood, lymph, and interstitial fluid. Water plays a crucial role in maintaining the body's temperature, transporting nutrients and oxygen to cells, removing waste products, and lubricating joints. It also helps to regulate blood pressure and prevent dehydration, which can lead to a range of health problems. In medical settings, water is often used as a means of hydration therapy for patients who are dehydrated or have fluid imbalances. It may also be used as a diluent for medications or as a component of intravenous fluids. Overall, water is an essential component of human health and plays a critical role in maintaining the body's normal functions.
Muramidase is an enzyme that is involved in the degradation of peptidoglycan, a major component of bacterial cell walls. It is also known as lysozyme or muramidase lysozyme. The enzyme cleaves the bond between the N-acetylglucosamine and N-acetylmuramic acid residues in the peptidoglycan chain, leading to the breakdown of the cell wall and ultimately the death of the bacterium. Muramidase is found in various organisms, including humans, and is used as an antimicrobial agent in some medications. It is also used in laboratory research to study bacterial cell wall structure and function.
Apoproteins are proteins that are associated with lipids (fats) in the bloodstream. They play a crucial role in the transport and metabolism of lipids in the body. There are several different types of apolipoproteins, each with a specific function. Apolipoproteins are found in lipoprotein particles, which are complexes of lipids and proteins that transport lipids through the bloodstream. The different types of apolipoproteins are associated with different types of lipoproteins, such as low-density lipoprotein (LDL) and high-density lipoprotein (HDL). Apolipoproteins are important for maintaining healthy lipid levels in the body. For example, HDL, which is often referred to as "good cholesterol," contains the apolipoprotein A-I, which helps to remove excess cholesterol from the bloodstream and transport it back to the liver for processing and elimination. Abnormal levels of apolipoproteins can be associated with various health conditions, such as high cholesterol, heart disease, and diabetes. Therefore, measuring levels of apolipoproteins can be an important part of diagnosing and managing these conditions.
In the medical field, hydrogen is not typically used as a standalone treatment or medication. However, there is some research being conducted on the potential therapeutic uses of hydrogen gas (H2) in various medical conditions. One area of interest is in the treatment of oxidative stress and inflammation, which are underlying factors in many chronic diseases such as cancer, diabetes, and neurodegenerative disorders. Hydrogen gas has been shown to have antioxidant and anti-inflammatory effects, and some studies have suggested that it may have potential as a therapeutic agent in these conditions. Another area of research is in the treatment of traumatic brain injury (TBI). Hydrogen gas has been shown to reduce oxidative stress and inflammation in animal models of TBI, and some studies have suggested that it may have potential as a neuroprotective agent in humans. However, it's important to note that the use of hydrogen gas in medicine is still in the early stages of research, and more studies are needed to fully understand its potential therapeutic benefits and risks. As such, hydrogen gas should not be used as a substitute for conventional medical treatments without the guidance of a qualified healthcare professional.
Prions are infectious agents that consist solely of protein, without any genetic material such as DNA or RNA. They are responsible for a group of rare and fatal neurodegenerative diseases, including Creutzfeldt-Jakob disease (CJD) and kuru in humans, and scrapie in sheep. Prions are unique in that they can cause normal proteins in the body to misfold and adopt the same abnormal shape, leading to the accumulation of these misfolded proteins in the brain and other tissues. This accumulation of misfolded proteins is what causes the damage and death of brain cells in prion diseases. Prions are highly resistant to heat, radiation, and many disinfectants, making them difficult to eliminate from contaminated materials. They can also be transmitted through contact with infected tissues or bodily fluids, or through contaminated food or medical equipment.
Guanidine is a chemical compound that is commonly used in the medical field as a medication and a research tool. It is a white, crystalline solid that is soluble in water and has a bitter taste. Guanidine is used to treat a variety of conditions, including hypertension (high blood pressure), congestive heart failure, and certain types of kidney disease. It works by relaxing blood vessels and reducing the workload on the heart, which can help to lower blood pressure and improve blood flow. Guanidine is also used in research to study the structure and function of proteins, and to develop new drugs and therapies.
Bacteriorhodopsins are a family of light-sensitive proteins found in the membranes of certain bacteria, such as Halobacterium salinarum. They are also known as light-driven proton pumps because they use the energy from light to pump protons across the membrane, creating a proton gradient that can be used to power various cellular processes. In the medical field, bacteriorhodopsins have been studied for their potential use in a variety of applications, including as optogenetic tools for controlling the activity of neurons in the brain, as sensors for detecting environmental pollutants, and as components of biofuel cells that can convert light energy into electrical energy. Bacteriorhodopsins have also been used in the development of new drugs and therapies. For example, researchers have developed a bacteriorhodopsin-based drug that can be used to treat glaucoma by increasing the production of aqueous humor in the eye. Additionally, bacteriorhodopsins have been used to develop new types of solar cells that can convert light energy into electrical energy more efficiently than traditional solar cells.
In the medical field, Schiff bases are a class of organic compounds that are formed by the condensation reaction between an amine and a carbonyl compound. These compounds are named after the German chemist Hugo Schiff, who first described their synthesis in the late 19th century. Schiff bases have a wide range of applications in medicine, including as antibacterial, antifungal, and antiviral agents. They are also used as ligands in metal complexes, which can be used in the treatment of various diseases, such as cancer and inflammatory disorders. One of the most well-known Schiff bases in medicine is metronidazole, which is used to treat infections caused by anaerobic bacteria and protozoa. Other examples of Schiff bases with medical applications include thiosemicarbazones, which are used to treat cancer, and salicylaldehyde Schiff bases, which have anti-inflammatory properties. Overall, Schiff bases are an important class of compounds in the medical field, with a wide range of potential applications in the treatment of various diseases and conditions.
Bacterial proteins are proteins that are synthesized by bacteria. They are essential for the survival and function of bacteria, and play a variety of roles in bacterial metabolism, growth, and pathogenicity. Bacterial proteins can be classified into several categories based on their function, including structural proteins, metabolic enzymes, regulatory proteins, and toxins. Structural proteins provide support and shape to the bacterial cell, while metabolic enzymes are involved in the breakdown of nutrients and the synthesis of new molecules. Regulatory proteins control the expression of other genes, and toxins can cause damage to host cells and tissues. Bacterial proteins are of interest in the medical field because they can be used as targets for the development of antibiotics and other antimicrobial agents. They can also be used as diagnostic markers for bacterial infections, and as vaccines to prevent bacterial diseases. Additionally, some bacterial proteins have been shown to have therapeutic potential, such as enzymes that can break down harmful substances in the body or proteins that can stimulate the immune system.
Amyloid is a type of protein that is abnormal and forms deposits in tissues throughout the body. These deposits are made up of fibrils, which are long, twisted strands of protein. Amyloidosis is a disease that occurs when amyloid fibrils build up in tissues, leading to damage and dysfunction. There are many different types of amyloidosis, which can affect different organs and tissues in the body. Some types of amyloidosis are inherited, while others are acquired. Treatment for amyloidosis depends on the specific type and severity of the disease.
Deuterium is a stable isotope of hydrogen that has one extra neutron in its nucleus compared to the most common isotope of hydrogen, protium. In the medical field, deuterium is sometimes used as a tracer in nuclear medicine imaging studies. For example, deuterium oxide (heavy water) can be used to label certain molecules, such as glucose or amino acids, which can then be injected into the body and imaged using positron emission tomography (PET) or single-photon emission computed tomography (SPECT). This can help doctors to visualize the uptake and metabolism of these molecules in different tissues and organs, which can be useful for diagnosing and monitoring various medical conditions. Deuterium is also used in some types of radiation therapy, where it is used to replace hydrogen atoms in certain molecules to make them more radioactive, allowing them to be targeted to specific cancer cells.
In the medical field, a peptide fragment refers to a short chain of amino acids that are derived from a larger peptide or protein molecule. Peptide fragments can be generated through various techniques, such as enzymatic digestion or chemical cleavage, and are often used in diagnostic and therapeutic applications. Peptide fragments can be used as biomarkers for various diseases, as they may be present in the body at elevated levels in response to specific conditions. For example, certain peptide fragments have been identified as potential biomarkers for cancer, neurodegenerative diseases, and cardiovascular disease. In addition, peptide fragments can be used as therapeutic agents themselves. For example, some peptide fragments have been shown to have anti-inflammatory or anti-cancer properties, and are being investigated as potential treatments for various diseases. Overall, peptide fragments play an important role in the medical field, both as diagnostic tools and as potential therapeutic agents.
In the medical field, macromolecular substances refer to large molecules that are composed of repeating units, such as proteins, carbohydrates, lipids, and nucleic acids. These molecules are essential for many biological processes, including cell signaling, metabolism, and structural support. Macromolecular substances are typically composed of thousands or even millions of atoms, and they can range in size from a few nanometers to several micrometers. They are often found in the form of fibers, sheets, or other complex structures, and they can be found in a variety of biological tissues and fluids. Examples of macromolecular substances in the medical field include: - Proteins: These are large molecules composed of amino acids that are involved in a wide range of biological functions, including enzyme catalysis, structural support, and immune response. - Carbohydrates: These are molecules composed of carbon, hydrogen, and oxygen atoms that are involved in energy storage, cell signaling, and structural support. - Lipids: These are molecules composed of fatty acids and glycerol that are involved in energy storage, cell membrane structure, and signaling. - Nucleic acids: These are molecules composed of nucleotides that are involved in genetic information storage and transfer. Macromolecular substances are important for many medical applications, including drug delivery, tissue engineering, and gene therapy. Understanding the structure and function of these molecules is essential for developing new treatments and therapies for a wide range of diseases and conditions.
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of rare and fatal neurological disorders that are caused by abnormal proteins called prions. These diseases are characterized by the accumulation of misfolded prion proteins in the brain, leading to the destruction of brain tissue and the development of spongy holes, or vacuoles, in the brain. There are several different types of prion diseases, including Creutzfeldt-Jakob disease (CJD), kuru, Gerstmann-Sträussler-Scheinker syndrome (GSS), fatal familial insomnia (FFI), and variant Creutzfeldt-Jakob disease (vCJD). These diseases can affect humans and other animals, including cattle, sheep, and deer. Prion diseases are infectious, meaning that they can be transmitted from one individual to another through contact with infected tissues or bodily fluids. They are also unique in that they are not caused by viruses or bacteria, but rather by abnormal proteins. There is currently no cure for prion diseases, and treatment is focused on managing symptoms and providing supportive care.
DNA, or deoxyribonucleic acid, is a molecule that carries genetic information in living organisms. It is composed of four types of nitrogen-containing molecules called nucleotides, which are arranged in a specific sequence to form the genetic code. In the medical field, DNA is often studied as a tool for understanding and diagnosing genetic disorders. Genetic disorders are caused by changes in the DNA sequence that can affect the function of genes, leading to a variety of health problems. By analyzing DNA, doctors and researchers can identify specific genetic mutations that may be responsible for a particular disorder, and develop targeted treatments or therapies to address the underlying cause of the condition. DNA is also used in forensic science to identify individuals based on their unique genetic fingerprint. This is because each person's DNA sequence is unique, and can be used to distinguish one individual from another. DNA analysis is also used in criminal investigations to help solve crimes by linking DNA evidence to suspects or victims.
In the medical field, protons are subatomic particles that have a positive charge and are found in the nucleus of an atom. They are one of the two types of particles that make up atomic nuclei, the other being neutrons, which have no charge. Protons are important in medical applications because they can be used in a type of radiation therapy called proton therapy. Proton therapy is a type of cancer treatment that uses beams of protons to target and destroy cancer cells while minimizing damage to surrounding healthy tissue. This is because protons have a unique property called the Bragg peak, which allows them to deposit most of their energy at a specific depth in the body before coming to a stop. This makes proton therapy particularly effective for treating certain types of cancer, such as brain tumors and pediatric cancers.
Chymotrypsin is a digestive enzyme that is produced by the pancreas and secreted into the small intestine. It is a protease enzyme that breaks down proteins into smaller peptides and amino acids. Chymotrypsin is particularly effective at breaking down proteins that contain aromatic amino acids such as tryptophan, tyrosine, and phenylalanine. In the medical field, chymotrypsin is used to treat a variety of conditions, including: 1. Pancreatitis: Chymotrypsin is used to help break down the excess enzymes in the pancreas that can cause inflammation and damage to the pancreas. 2. Gallstones: Chymotrypsin is used to dissolve gallstones that are composed of cholesterol. 3. Inflammatory bowel disease: Chymotrypsin is used to help reduce inflammation in the digestive tract. 4. Cancer: Chymotrypsin is being studied as a potential treatment for certain types of cancer, including breast cancer and prostate cancer. Chymotrypsin is usually administered as a medication in the form of a tablet or injection. It is important to note that chymotrypsin can have side effects, including nausea, vomiting, and diarrhea, and should only be used under the guidance of a healthcare professional.
In the medical field, amides are a class of organic compounds that contain a nitrogen atom bonded to two carbon atoms. They are commonly used as drugs and are often referred to as "amide derivatives." One example of an amide derivative used in medicine is acetaminophen, which is commonly sold under the brand name Tylenol. It is used to relieve pain and reduce fever. Another example is aspirin, which is also an amide derivative and is used to relieve pain, reduce fever, and thin the blood. Amides can also be used as local anesthetics, such as lidocaine, which is used to numb the skin and nerves during medical procedures. They can also be used as muscle relaxants, such as succinylcholine, which is used to relax muscles during surgery. Overall, amides play an important role in medicine as they have a wide range of therapeutic applications and are often used to treat various medical conditions.
Cysteine is an amino acid that is essential for the proper functioning of the human body. It is a sulfur-containing amino acid that is involved in the formation of disulfide bonds, which are important for the structure and function of many proteins. Cysteine is also involved in the detoxification of harmful substances in the body, and it plays a role in the production of glutathione, a powerful antioxidant. In the medical field, cysteine is used to treat a variety of conditions, including respiratory infections, kidney stones, and cataracts. It is also used as a dietary supplement to support overall health and wellness.
In the medical field, a mutant protein refers to a protein that has undergone a genetic mutation, resulting in a change in its structure or function. Mutations can occur in the DNA sequence that codes for a protein, leading to the production of a protein with a different amino acid sequence than the normal, or wild-type, protein. Mutant proteins can be associated with a variety of medical conditions, including genetic disorders, cancer, and neurodegenerative diseases. For example, mutations in the BRCA1 and BRCA2 genes can increase the risk of breast and ovarian cancer, while mutations in the huntingtin gene can cause Huntington's disease. In some cases, mutant proteins can be targeted for therapeutic intervention. For example, drugs that inhibit the activity of mutant proteins or promote the degradation of mutant proteins may be used to treat certain types of cancer or other diseases.
Molecular chaperones are a class of proteins that assist in the folding, assembly, and transport of other proteins within cells. They play a crucial role in maintaining cellular homeostasis and preventing the accumulation of misfolded or aggregated proteins, which can lead to various diseases such as neurodegenerative disorders, cancer, and certain types of infections. Molecular chaperones function by binding to nascent or partially folded proteins, preventing them from aggregating and promoting their proper folding. They also assist in the assembly of multi-subunit proteins, such as enzymes and ion channels, by ensuring that the individual subunits are correctly folded and assembled into a functional complex. There are several types of molecular chaperones, including heat shock proteins (HSPs), chaperonins, and small heat shock proteins (sHSPs). HSPs are induced in response to cellular stress, such as heat shock or oxidative stress, and are involved in the refolding of misfolded proteins. Chaperonins, on the other hand, are found in the cytosol and the endoplasmic reticulum and are involved in the folding of large, complex proteins. sHSPs are found in the cytosol and are involved in the stabilization of unfolded proteins and preventing their aggregation. Overall, molecular chaperones play a critical role in maintaining protein homeostasis within cells and are an important target for the development of new therapeutic strategies for various diseases.
Trypsin is a proteolytic enzyme that is produced by the pancreas and is responsible for breaking down proteins into smaller peptides and amino acids. It is a serine protease that cleaves peptide bonds on the carboxyl side of lysine and arginine residues. Trypsin is an important digestive enzyme that helps to break down dietary proteins into smaller peptides and amino acids that can be absorbed and used by the body. It is also used in medical research and in the development of diagnostic tests and therapeutic agents.
Amino acids are organic compounds that are the building blocks of proteins. They are composed of an amino group (-NH2), a carboxyl group (-COOH), and a side chain (R group) that varies in size and structure. There are 20 different amino acids that are commonly found in proteins, each with a unique side chain that gives it distinct chemical and physical properties. In the medical field, amino acids are important for a variety of functions, including the synthesis of proteins, enzymes, and hormones. They are also involved in energy metabolism and the maintenance of healthy tissues. Deficiencies in certain amino acids can lead to a range of health problems, including muscle wasting, anemia, and neurological disorders. In some cases, amino acids may be prescribed as supplements to help treat these conditions or to support overall health and wellness.
In the medical field, ions are charged particles that are either positively or negatively charged. They are formed when an atom gains or loses electrons, and they play a crucial role in many bodily functions. For example, ions such as sodium, potassium, calcium, and chloride are essential for maintaining the proper balance of fluids in the body, which is necessary for proper nerve and muscle function. Imbalances in these ions can lead to a variety of medical conditions, such as hypertension, heart disease, and muscle cramps. In addition, ions are also important in the transmission of nerve impulses and the functioning of the immune system. They are also used in medical treatments such as electrotherapy and iontophoresis, which involve the application of electrical currents to the body to treat various conditions.
Hemeproteins are a class of proteins that contain a heme group, which is a complex of iron and porphyrin. Hemeproteins are found in many organisms and play important roles in a variety of biological processes, including oxygen transport, energy metabolism, and detoxification. The most well-known hemeprotein is hemoglobin, which is found in red blood cells and is responsible for carrying oxygen from the lungs to the body's tissues. Hemoglobin is composed of four subunits, each of which contains a heme group. The iron atom in the heme group can bind to oxygen molecules, allowing hemoglobin to transport oxygen throughout the body. Other examples of hemeproteins include myoglobin, which is found in muscle tissue and stores oxygen for use during periods of high physical activity, and cytochrome P450 enzymes, which are involved in the metabolism of drugs and other xenobiotics. Hemeproteins are important for many biological processes and are the subject of ongoing research in the medical field.
Adenosine triphosphate (ATP) is a molecule that serves as the primary energy currency in living cells. It is composed of three phosphate groups attached to a ribose sugar and an adenine base. In the medical field, ATP is essential for many cellular processes, including muscle contraction, nerve impulse transmission, and the synthesis of macromolecules such as proteins and nucleic acids. ATP is produced through cellular respiration, which involves the breakdown of glucose and other molecules to release energy that is stored in the bonds of ATP. Disruptions in ATP production or utilization can lead to a variety of medical conditions, including muscle weakness, fatigue, and neurological disorders. In addition, ATP is often used as a diagnostic tool in medical testing, as levels of ATP can be measured in various bodily fluids and tissues to assess cellular health and function.
Heme is a complex organic molecule that contains iron and is a vital component of hemoglobin, myoglobin, and other proteins involved in oxygen transport and storage in living organisms. It is also a component of various enzymes involved in metabolism and detoxification processes. In the medical field, heme is often used as a diagnostic tool to detect and monitor certain medical conditions, such as anemia (a deficiency of red blood cells or hemoglobin), liver disease (which can affect heme synthesis), and certain types of cancer (which can produce abnormal heme molecules). Heme is also used in the production of certain medications, such as heme-based oxygen carriers for use in patients with sickle cell disease or other conditions that affect oxygen transport. Additionally, heme is a component of some dietary supplements and is sometimes used to treat certain types of anemia.
Urea is a chemical compound that is produced in the liver as a waste product of protein metabolism. It is then transported to the kidneys, where it is filtered out of the blood and excreted in the urine. In the medical field, urea is often used as a diagnostic tool to measure kidney function. High levels of urea in the blood can be a sign of kidney disease or other medical conditions, while low levels may indicate malnutrition or other problems. Urea is also used as a source of nitrogen in fertilizers and as a raw material in the production of plastics and other chemicals.
Membrane proteins are proteins that are embedded within the lipid bilayer of a cell membrane. They play a crucial role in regulating the movement of substances across the membrane, as well as in cell signaling and communication. There are several types of membrane proteins, including integral membrane proteins, which span the entire membrane, and peripheral membrane proteins, which are only in contact with one or both sides of the membrane. Membrane proteins can be classified based on their function, such as transporters, receptors, channels, and enzymes. They are important for many physiological processes, including nutrient uptake, waste elimination, and cell growth and division.
Lysine is an essential amino acid that is required for the growth and maintenance of tissues in the human body. It is one of the nine essential amino acids that cannot be synthesized by the body and must be obtained through the diet. Lysine plays a crucial role in the production of proteins, including enzymes, hormones, and antibodies. It is also involved in the absorption of calcium and the production of niacin, a B vitamin that is important for energy metabolism and the prevention of pellagra. In the medical field, lysine is used to treat and prevent various conditions, including: 1. Herpes simplex virus (HSV): Lysine supplements have been shown to reduce the frequency and severity of outbreaks of HSV-1 and HSV-2, which cause cold sores and genital herpes, respectively. 2. Cold sores: Lysine supplements can help reduce the frequency and severity of cold sore outbreaks by inhibiting the replication of the herpes simplex virus. 3. Depression: Lysine has been shown to increase levels of serotonin, a neurotransmitter that regulates mood, in the brain. 4. Hair loss: Lysine is important for the production of hair, and deficiency in lysine has been linked to hair loss. 5. Wound healing: Lysine is involved in the production of collagen, a protein that is important for wound healing. Overall, lysine is an important nutrient that plays a crucial role in many aspects of human health and is used in the treatment and prevention of various medical conditions.
In the medical field, the term "Cytochrome c Group" refers to a family of heme-containing proteins that are involved in electron transfer reactions in the mitochondria of cells. These proteins play a crucial role in the electron transport chain, which is responsible for generating ATP, the energy currency of the cell. Cytochrome c is a small, water-soluble protein that is released from the mitochondria during apoptosis, a programmed cell death process. The release of cytochrome c from the mitochondria is a key event in the initiation of apoptosis, and it has been implicated in a number of diseases, including cancer, neurodegenerative disorders, and cardiovascular disease. Other members of the cytochrome c group include cytochrome b, cytochrome c1, and cytochrome oxidase. These proteins work together to transfer electrons from one molecule to another, ultimately leading to the reduction of oxygen to water. Any disruption in the function of these proteins can lead to a buildup of reactive oxygen species, which can damage cellular components and contribute to disease.
Recombinant fusion proteins are proteins that are produced by combining two or more genes in a single molecule. These proteins are typically created using genetic engineering techniques, such as recombinant DNA technology, to insert one or more genes into a host organism, such as bacteria or yeast, which then produces the fusion protein. Fusion proteins are often used in medical research and drug development because they can have unique properties that are not present in the individual proteins that make up the fusion. For example, a fusion protein might be designed to have increased stability, improved solubility, or enhanced targeting to specific cells or tissues. Recombinant fusion proteins have a wide range of applications in medicine, including as therapeutic agents, diagnostic tools, and research reagents. Some examples of recombinant fusion proteins used in medicine include antibodies, growth factors, and cytokines.
Aspartic acid is an amino acid that is naturally occurring in the human body. It is a non-essential amino acid, meaning that it can be synthesized by the body from other compounds and does not need to be obtained through the diet. Aspartic acid is found in high concentrations in the brain and spinal cord, and it plays a role in various physiological processes, including the production of neurotransmitters and the regulation of acid-base balance in the body. In the medical field, aspartic acid is sometimes used as a diagnostic tool to measure the function of the liver and kidneys, as well as to monitor the progression of certain diseases, such as cancer and HIV. It is also used as a dietary supplement in some cases.
Monoclonal antibodies (mAbs) are laboratory-made proteins that can mimic the immune system's ability to fight off harmful pathogens, such as viruses and bacteria. They are produced by genetically engineering cells to produce large quantities of a single type of antibody, which is specific to a particular antigen (a molecule that triggers an immune response). In the medical field, monoclonal antibodies are used to treat a variety of conditions, including cancer, autoimmune diseases, and infectious diseases. They can be administered intravenously, intramuscularly, or subcutaneously, depending on the condition being treated. Monoclonal antibodies work by binding to specific antigens on the surface of cells or pathogens, marking them for destruction by the immune system. They can also block the activity of specific molecules involved in disease processes, such as enzymes or receptors. Overall, monoclonal antibodies have revolutionized the treatment of many diseases, offering targeted and effective therapies with fewer side effects than traditional treatments.
Zinc is a chemical element that is essential for human health. In the medical field, zinc is used in a variety of ways, including as a supplement to treat and prevent certain health conditions. Zinc is involved in many important bodily functions, including immune system function, wound healing, and DNA synthesis. It is also important for the proper functioning of the senses of taste and smell. Zinc deficiency can lead to a range of health problems, including impaired immune function, delayed wound healing, and impaired growth and development in children. Zinc supplements are often recommended for people who are at risk of zinc deficiency, such as pregnant and breastfeeding women, people with certain medical conditions, and people who follow a vegetarian or vegan diet. In addition to its use as a supplement, zinc is also used in some medications, such as those used to treat acne and the common cold. It is also used in some over-the-counter products, such as antacids and nasal sprays. Overall, zinc is an important nutrient that plays a vital role in maintaining good health.
Serum Albumin, Bovine is a type of albumin, which is a type of protein found in the blood plasma of mammals. It is derived from the blood of cows and is used as a source of albumin for medical purposes. Albumin is an important protein in the body that helps to maintain the osmotic pressure of blood and transport various substances, such as hormones, drugs, and fatty acids, throughout the body. It is often used as a plasma expander in patients who have lost a significant amount of blood or as a replacement for albumin in patients with liver disease or other conditions that affect albumin production.
Hemoglobins are a group of proteins found in red blood cells (erythrocytes) that are responsible for carrying oxygen from the lungs to the body's tissues and carbon dioxide from the tissues back to the lungs. Hemoglobin is composed of four subunits, each of which contains a heme group that binds to oxygen. The oxygen binds to the iron atom in the heme group, allowing the hemoglobin to transport oxygen throughout the body. Hemoglobin also plays a role in regulating the pH of the blood and in the immune response. Abnormalities in hemoglobin can lead to various medical conditions, such as anemia, sickle cell disease, and thalassemia.
Calcium is a chemical element with the symbol Ca and atomic number 20. It is a vital mineral for the human body and is essential for many bodily functions, including bone health, muscle function, nerve transmission, and blood clotting. In the medical field, calcium is often used to diagnose and treat conditions related to calcium deficiency or excess. For example, low levels of calcium in the blood (hypocalcemia) can cause muscle cramps, numbness, and tingling, while high levels (hypercalcemia) can lead to kidney stones, bone loss, and other complications. Calcium supplements are often prescribed to people who are at risk of developing calcium deficiency, such as older adults, vegetarians, and people with certain medical conditions. However, it is important to note that excessive calcium intake can also be harmful, and it is important to follow recommended dosages and consult with a healthcare provider before taking any supplements.
In the medical field, carrier proteins are proteins that transport molecules across cell membranes or within cells. These proteins bind to specific molecules, such as hormones, nutrients, or waste products, and facilitate their movement across the membrane or within the cell. Carrier proteins play a crucial role in maintaining the proper balance of molecules within cells and between cells. They are involved in a wide range of physiological processes, including nutrient absorption, hormone regulation, and waste elimination. There are several types of carrier proteins, including facilitated diffusion carriers, active transport carriers, and ion channels. Each type of carrier protein has a specific function and mechanism of action. Understanding the role of carrier proteins in the body is important for diagnosing and treating various medical conditions, such as genetic disorders, metabolic disorders, and neurological disorders.
Plant proteins are proteins that are derived from plants. They are an important source of dietary protein for many people and are a key component of a healthy diet. Plant proteins are found in a wide variety of plant-based foods, including legumes, nuts, seeds, grains, and vegetables. They are an important source of essential amino acids, which are the building blocks of proteins and are necessary for the growth and repair of tissues in the body. Plant proteins are also a good source of fiber, vitamins, and minerals, and are generally lower in saturated fat and cholesterol than animal-based proteins. In the medical field, plant proteins are often recommended as part of a healthy diet for people with certain medical conditions, such as heart disease, diabetes, and high blood pressure.
Polydeoxyribonucleotides, also known as poly(dNTPs), are polymers of deoxyribonucleotides, which are the building blocks of DNA. They are composed of a sugar molecule (deoxyribose), a phosphate group, and a nitrogenous base (adenine, thymine, cytosine, or guanine). In the medical field, poly(dNTPs) are commonly used as a substrate in DNA polymerase reactions, which are essential for DNA replication and repair. They are also used in various molecular biology techniques, such as polymerase chain reaction (PCR), DNA sequencing, and DNA synthesis. Poly(dNTPs) are available in different concentrations and purities, and their selection depends on the specific application and experimental requirements.
In the medical field, "iron" refers to a mineral that is essential for the production of red blood cells, which carry oxygen throughout the body. Iron is also important for the proper functioning of the immune system, metabolism, and energy production. Iron deficiency is a common condition that can lead to anemia, a condition in which the body does not have enough red blood cells to carry oxygen to the body's tissues. Symptoms of iron deficiency anemia may include fatigue, weakness, shortness of breath, and pale skin. Iron supplements are often prescribed to treat iron deficiency anemia, and dietary changes may also be recommended to increase iron intake. However, it is important to note that excessive iron intake can also be harmful, so it is important to follow the recommended dosage and consult with a healthcare provider before taking any iron supplements.
Saccharomyces cerevisiae proteins are proteins that are produced by the yeast species Saccharomyces cerevisiae. This yeast is commonly used in the production of bread, beer, and wine, as well as in scientific research. In the medical field, S. cerevisiae proteins have been studied for their potential use in the treatment of various diseases, including cancer, diabetes, and neurodegenerative disorders. Some S. cerevisiae proteins have also been shown to have anti-inflammatory and immunomodulatory effects, making them of interest for the development of new therapies.
In the medical field, disulfides refer to chemical compounds that contain two sulfur atoms connected by a single bond. Disulfides are commonly found in proteins, where they play an important role in maintaining the structure and function of the protein. One of the most well-known examples of a disulfide is the cystine molecule, which is composed of two cysteine amino acids that are linked together by a disulfide bond. Disulfide bonds are important for the proper folding and stability of proteins, and they can also play a role in the function of the protein. Disulfides can also be found in other types of molecules, such as lipids and carbohydrates. In these cases, disulfides may play a role in the structure and function of the molecule, or they may be involved in signaling pathways within the body. Overall, disulfides are an important class of chemical compounds that play a variety of roles in the body, including the maintenance of protein structure and function, and the regulation of signaling pathways.
Trifluoroethanol, also known as 2,2,2-trifluoroethanol or TFE, is a colorless, volatile liquid with a sweet odor. It is a polar solvent that is commonly used in the medical field as a chemical reagent and a solvent for various organic compounds. In the medical field, trifluoroethanol is used in a variety of applications, including as a solvent for the extraction of proteins and other biological molecules, as a denaturant for proteins, and as a stabilizer for enzymes. It is also used as a solvent for the purification of certain drugs and as a component in the production of certain pharmaceuticals. Trifluoroethanol is generally considered to be safe for use in the medical field, although it can be toxic in high concentrations. It is important to handle it with care and to follow proper safety procedures when working with this chemical.
Magnesium is a mineral that is essential for many bodily functions. It is involved in over 300 enzymatic reactions in the body, including the production of energy, the synthesis of proteins and DNA, and the regulation of muscle and nerve function. In the medical field, magnesium is used to treat a variety of conditions, including: 1. Hypomagnesemia: A deficiency of magnesium in the blood. This can cause symptoms such as muscle cramps, spasms, and seizures. 2. Cardiac arrhythmias: Abnormal heart rhythms that can be caused by low levels of magnesium. 3. Pre-eclampsia: A condition that can occur during pregnancy and is characterized by high blood pressure and protein in the urine. Magnesium supplementation may be used to treat this condition. 4. Chronic kidney disease: Magnesium is often lost in the urine of people with chronic kidney disease, and supplementation may be necessary to maintain adequate levels. 5. Alcohol withdrawal: Magnesium supplementation may be used to treat symptoms of alcohol withdrawal, such as tremors and seizures. 6. Muscle spasms: Magnesium can help to relax muscles and relieve spasms. 7. Anxiety and depression: Some studies have suggested that magnesium supplementation may help to reduce symptoms of anxiety and depression. Magnesium is available in various forms, including oral tablets, capsules, and intravenous solutions. It is important to note that high levels of magnesium can also be toxic, so it is important to use magnesium supplements under the guidance of a healthcare provider.
Escherichia coli (E. coli) is a type of bacteria that is commonly found in the human gut. E. coli proteins are proteins that are produced by E. coli bacteria. These proteins can have a variety of functions, including helping the bacteria to survive and thrive in the gut, as well as potentially causing illness in humans. In the medical field, E. coli proteins are often studied as potential targets for the development of new treatments for bacterial infections. For example, some E. coli proteins are involved in the bacteria's ability to produce toxins that can cause illness in humans, and researchers are working to develop drugs that can block the activity of these proteins in order to prevent or treat E. coli infections. E. coli proteins are also used in research to study the biology of the bacteria and to understand how it interacts with the human body. For example, researchers may use E. coli proteins as markers to track the growth and spread of the bacteria in the gut, or they may use them to study the mechanisms by which the bacteria causes illness. Overall, E. coli proteins are an important area of study in the medical field, as they can provide valuable insights into the biology of this important bacterium and may have potential applications in the treatment of bacterial infections.
In the medical field, lipid bilayers refer to the two layers of phospholipid molecules that form the basic structure of cell membranes. The lipid bilayer is composed of a hydrophilic (water-loving) head and a hydrophobic (water-fearing) tail. The hydrophilic heads face outward, towards the aqueous environment of the cell, while the hydrophobic tails face inward, towards each other. This arrangement creates a barrier that separates the inside of the cell from the outside environment, while also allowing for the selective passage of molecules in and out of the cell. The lipid bilayer is essential for maintaining the integrity and function of cells, and is involved in a wide range of cellular processes, including cell signaling, metabolism, and transport.
Oligodeoxyribonucleotides (ODNs) are short chains of DNA or RNA that are synthesized in the laboratory. They are typically used as tools in molecular biology research, as well as in therapeutic applications such as gene therapy. ODNs can be designed to bind to specific DNA or RNA sequences, and can be used to modulate gene expression or to introduce genetic changes into cells. They can also be used as primers in PCR (polymerase chain reaction) to amplify specific DNA sequences. In the medical field, ODNs are being studied for their potential use in treating a variety of diseases, including cancer, viral infections, and genetic disorders. For example, ODNs can be used to silence specific genes that are involved in disease progression, or to stimulate the immune system to attack cancer cells.
Proline is an amino acid that is commonly found in proteins. It is a non-essential amino acid, meaning that it can be synthesized by the body from other amino acids. In the medical field, proline is often used as a diagnostic tool to measure the levels of certain enzymes in the body, such as alanine transaminase (ALT) and aspartate transaminase (AST). These enzymes are released into the bloodstream when the liver is damaged, so elevated levels of proline can indicate liver disease. Proline is also used in the treatment of certain medical conditions, such as Peyronie's disease, which is a condition that causes curvature of the penis. Proline has been shown to help improve the flexibility of the penis and reduce the curvature associated with Peyronie's disease.
In the medical field, oligopeptides are short chains of amino acids that typically contain between two and 50 amino acids. They are often used in various medical applications due to their unique properties and potential therapeutic effects. One of the main benefits of oligopeptides is their ability to penetrate the skin and reach underlying tissues, making them useful in the development of topical treatments for a variety of conditions. For example, oligopeptides have been shown to improve skin elasticity, reduce the appearance of wrinkles, and promote the growth of new skin cells. Oligopeptides are also used in the development of medications for a variety of conditions, including osteoporosis, diabetes, and hypertension. They work by interacting with specific receptors in the body, which can help to regulate various physiological processes and improve overall health. Overall, oligopeptides are a promising area of research in the medical field, with potential applications in a wide range of therapeutic areas.
Micelles are small, spherical structures that form when surfactant molecules, such as phospholipids, are dissolved in water. In the medical field, micelles are often used as drug delivery systems to transport drugs across cell membranes and into cells. This is because the hydrophobic core of the micelle can encapsulate hydrophobic drugs, while the hydrophilic shell of the micelle can interact with water and other polar molecules. This allows the drug to be transported through the bloodstream and into cells, where it can be released and exert its therapeutic effect. Micelles are also used in various medical imaging techniques, such as magnetic resonance imaging (MRI), to enhance the contrast between different tissues in the body.
In the medical field, nucleotides are the building blocks of nucleic acids, which are the genetic material of cells. Nucleotides are composed of three components: a nitrogenous base, a pentose sugar, and a phosphate group. There are four nitrogenous bases in DNA: adenine (A), thymine (T), cytosine (C), and guanine (G). There are also four nitrogenous bases in RNA: adenine (A), uracil (U), cytosine (C), and guanine (G). The sequence of these nitrogenous bases determines the genetic information encoded in DNA and RNA.
Alanine is an amino acid that is a building block of proteins. It is an essential amino acid, meaning that it cannot be synthesized by the body and must be obtained through the diet. Alanine plays a number of important roles in the body, including: 1. Energy production: Alanine can be converted into glucose, which is a source of energy for the body. 2. Muscle function: Alanine is involved in the metabolism of muscle tissue and can help to prevent muscle damage. 3. Liver function: Alanine is an important component of the liver's detoxification process and can help to protect the liver from damage. 4. Acid-base balance: Alanine helps to regulate the body's acid-base balance by buffering excess acid in the blood. In the medical field, alanine is often used as a biomarker to assess liver function. Elevated levels of alanine in the blood can indicate liver damage or disease. Alanine is also used as a dietary supplement to support muscle growth and recovery.
RNA, or ribonucleic acid, is a type of nucleic acid that is involved in the process of protein synthesis in cells. It is composed of a chain of nucleotides, which are made up of a sugar molecule, a phosphate group, and a nitrogenous base. There are three types of RNA: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). In the medical field, RNA is often studied as a potential target for the development of new drugs and therapies. For example, some researchers are exploring the use of RNA interference (RNAi) to silence specific genes and treat diseases such as cancer and viral infections. Additionally, RNA is being studied as a potential biomarker for various diseases, as changes in the levels or structure of certain RNA molecules can indicate the presence of a particular condition.
Histidine is an amino acid that is naturally occurring in the human body. It is a building block of proteins and is essential for the proper functioning of many bodily processes. In the medical field, histidine is often used as a diagnostic tool to help diagnose certain medical conditions. For example, high levels of histidine in the blood can be a sign of a genetic disorder called histidinemia, which can cause a range of symptoms including intellectual disability, seizures, and liver problems. Histidine is also used in the treatment of certain medical conditions, such as acidosis, which is a condition in which the body's pH balance is disrupted.
Adenosine diphosphate (ADP) is a molecule that plays a crucial role in various metabolic processes in the body, particularly in the regulation of energy metabolism. It is a nucleotide that is composed of adenine, ribose, and two phosphate groups. In the medical field, ADP is often used as a diagnostic tool to assess the function of platelets, which are blood cells that play a critical role in blood clotting. ADP is a potent activator of platelets, and a decrease in platelet aggregation in response to ADP is often an indication of a bleeding disorder. ADP is also used in the treatment of various medical conditions, including heart disease, stroke, and migraines. For example, drugs that inhibit ADP receptors on platelets, such as clopidogrel and ticagrelor, are commonly used to prevent blood clots in patients with heart disease or stroke. Overall, ADP is a critical molecule in the regulation of energy metabolism and the function of platelets, and its role in the medical field is significant.
In the medical field, a protein subunit refers to a smaller, functional unit of a larger protein complex. Proteins are made up of chains of amino acids, and these chains can fold into complex three-dimensional structures that perform a wide range of functions in the body. Protein subunits are often formed when two or more protein chains come together to form a larger complex. These subunits can be identical or different, and they can interact with each other in various ways to perform specific functions. For example, the protein hemoglobin, which carries oxygen in red blood cells, is made up of four subunits: two alpha chains and two beta chains. Each of these subunits has a specific structure and function, and they work together to form a functional hemoglobin molecule. In the medical field, understanding the structure and function of protein subunits is important for developing treatments for a wide range of diseases and conditions, including cancer, neurological disorders, and infectious diseases.
Gramicidin is a type of antibiotic that is derived from a soil bacterium called Bacillus brevis. It is a polypeptide antibiotic that is effective against a wide range of gram-positive bacteria, including Staphylococcus aureus, Streptococcus pyogenes, and Bacillus anthracis. Gramicidin works by disrupting the cell membrane of bacteria, causing it to leak and eventually leading to cell death. It is often used topically to treat skin infections, such as impetigo and cellulitis, and is also used to treat certain types of pneumonia and meningitis. However, gramicidin is not effective against gram-negative bacteria and can cause side effects such as allergic reactions and kidney damage when used in high doses.
Adenosine triphosphatases (ATPases) are a group of enzymes that hydrolyze adenosine triphosphate (ATP) to adenosine diphosphate (ADP) and inorganic phosphate (Pi). These enzymes play a crucial role in many cellular processes, including energy production, muscle contraction, and ion transport. In the medical field, ATPases are often studied in relation to various diseases and conditions. For example, mutations in certain ATPase genes have been linked to inherited disorders such as myopathy and neurodegenerative diseases. Additionally, ATPases are often targeted by drugs used to treat conditions such as heart failure, cancer, and autoimmune diseases. Overall, ATPases are essential enzymes that play a critical role in many cellular processes, and their dysfunction can have significant implications for human health.
DNA primers are short, single-stranded DNA molecules that are used in a variety of molecular biology techniques, including polymerase chain reaction (PCR) and DNA sequencing. They are designed to bind to specific regions of a DNA molecule, and are used to initiate the synthesis of new DNA strands. In PCR, DNA primers are used to amplify specific regions of DNA by providing a starting point for the polymerase enzyme to begin synthesizing new DNA strands. The primers are complementary to the target DNA sequence, and are added to the reaction mixture along with the DNA template, nucleotides, and polymerase enzyme. The polymerase enzyme uses the primers as a template to synthesize new DNA strands, which are then extended by the addition of more nucleotides. This process is repeated multiple times, resulting in the amplification of the target DNA sequence. DNA primers are also used in DNA sequencing to identify the order of nucleotides in a DNA molecule. In this application, the primers are designed to bind to specific regions of the DNA molecule, and are used to initiate the synthesis of short DNA fragments. The fragments are then sequenced using a variety of techniques, such as Sanger sequencing or next-generation sequencing. Overall, DNA primers are an important tool in molecular biology, and are used in a wide range of applications to study and manipulate DNA.
In the medical field, "DNA, Superhelical" refers to a type of DNA molecule that has a twisted or coiled structure, known as a double helix. The double helix is composed of two strands of nucleotides that are held together by hydrogen bonds between the nitrogenous bases. Superhelical DNA is characterized by an additional level of twist or winding around its axis, which is known as supercoiling. This supercoiling can occur in either a left-handed or right-handed direction, and it is thought to play a role in regulating gene expression and other cellular processes. Supercoiling can be induced by a variety of factors, including changes in temperature, pH, or the presence of certain enzymes. It can also be influenced by the presence of proteins that bind to the DNA and help to stabilize the superhelical structure. In medical research, supercoiled DNA is often used as a model system for studying the behavior of DNA under different conditions, as well as for developing new techniques for manipulating and analyzing DNA. It is also an important component of many genetic engineering and biotechnology applications.
Chromatin is a complex of DNA, RNA, and proteins that makes up the chromosomes in the nucleus of a cell. It plays a crucial role in regulating gene expression and maintaining the structure of the genome. In the medical field, chromatin is studied in relation to various diseases, including cancer, genetic disorders, and neurological conditions. For example, chromatin remodeling is a process that can alter the structure of chromatin and affect gene expression, and it has been implicated in the development of certain types of cancer. Additionally, chromatin-based therapies are being explored as potential treatments for diseases such as Alzheimer's and Parkinson's.
In the medical field, "Poly dA-dT" refers to a type of DNA polymer that is composed of alternating adenine (A) and thymine (T) nucleotides. This type of DNA is often used in laboratory experiments as a model system for studying DNA replication and repair mechanisms, as well as for developing new DNA-based technologies such as gene therapy and DNA sequencing. Poly dA-dT DNA is also known to form stable double-stranded structures that are resistant to degradation by nucleases, making it useful for a variety of applications in molecular biology and biotechnology.
Phenylalanine is an essential amino acid that is required for the production of proteins in the body. It is one of the building blocks of the protein called tyrosine, which is important for the production of hormones, neurotransmitters, and other important molecules in the body. Phenylalanine is also used in the production of certain neurotransmitters, including dopamine and norepinephrine, which play important roles in regulating mood, motivation, and other aspects of brain function. In the medical field, phenylalanine is often used as a dietary supplement to help individuals with certain medical conditions, such as phenylketonuria (PKU), which is a genetic disorder that affects the metabolism of phenylalanine. In PKU, the body is unable to properly break down phenylalanine, which can lead to a buildup of the amino acid in the blood and brain, causing damage to the brain and other organs. Phenylalanine is also used in some medications, such as certain antidepressants, to help regulate the production of neurotransmitters in the brain. However, it is important to note that phenylalanine can interact with other medications and may not be safe for everyone to take, so it is important to consult with a healthcare provider before taking any supplements or medications containing phenylalanine.
Adenylyl imidodiphosphate, also known as AMP-PPi or AMP-P2, is a molecule that plays a role in various cellular processes, including energy metabolism and signal transduction. It is a product of the reaction between adenosine monophosphate (AMP) and inorganic pyrophosphate (PPi), and is involved in the regulation of enzymes that catalyze the synthesis and breakdown of high-energy molecules such as ATP. In the medical field, AMP-PPi is sometimes used as a diagnostic tool to measure the activity of certain enzymes, and it has also been studied as a potential therapeutic target for the treatment of various diseases, including cancer and neurodegenerative disorders.
In the medical field, "salts" typically refers to compounds that contain ions of metals or other elements combined with non-metallic elements such as chlorine, sulfur, or phosphorus. These compounds are often used in various medical applications, including: 1. Electrolyte balance: Salts are essential for maintaining the balance of electrolytes in the body. Electrolytes are minerals that carry an electric charge and are necessary for many bodily functions, including muscle and nerve function, hydration, and acid-base balance. 2. Medications: Salts are often used as active ingredients in medications. For example, sodium chloride (table salt) is used as an ingredient in many over-the-counter pain relievers and cold medicines. 3. Antiseptics: Salts such as silver sulfadiazine are used as antiseptics to prevent infection in wounds. 4. Diuretics: Salts such as potassium chloride are used as diuretics to increase urine production and help remove excess fluids from the body. 5. Supplements: Salts such as magnesium sulfate are used as supplements to provide essential minerals that may be lacking in the diet. Overall, salts play an important role in many medical applications and are essential for maintaining proper bodily function.
Glycine is an amino acid that is essential for the proper functioning of the human body. It is a non-essential amino acid, meaning that the body can synthesize it from other compounds, but it is still important for various physiological processes. In the medical field, glycine is used as a dietary supplement to support muscle growth and recovery, as well as to improve sleep quality. It is also used in the treatment of certain medical conditions, such as liver disease, as it can help to reduce the buildup of toxins in the liver. Glycine is also used in the production of various medications, including antibiotics and tranquilizers. It has been shown to have a calming effect on the nervous system and may be used to treat anxiety and other mental health conditions. Overall, glycine is an important nutrient that plays a vital role in many physiological processes in the body.
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T4 Gene 32 Protein
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- Furin cleavage at the S1/S2 site may lead to conformational changes in the viral S protein that exposes the RBD and/or the S2 domain. (abcam.com)
- Consequently, during binding, S1 undergoes conformational rearrangement between two states, known as the up and down conformations. (abcam.com)
- We, therefore, need continuous descriptions of protein conformational space in the form of energy landscapes in order to properly understand their mechanisms of action. (europa.eu)
- 1980. The conformational stability of ribosomal protein L7/Ll2: The effects of pH, temperature and guani¬dinium chloride. (mote.org)
- Burger V., Arenas D., Stultz CM. A Structure-free Method for Quantifying Conformational Flexibility in proteins. (mit.edu)
- The high-affinity interaction of LF with pore-forming outer-membrane proteins (OMPs) of Gram-negative enterics, including Escherichia coli , is critical for the antimicrobial outcome of LF (Gado et al. (ift.org)
- 1979. The conformation of Escherichia coli ribosomal protein L7/Ll2 in solution: hydrodynamic, spectro¬scopic, and conformation prediction studies. (mote.org)
- These thermosensors are part of a regulatory network, such as the production of heat shock proteins mediated by sigma factor 32 (RpoH) in Escherichia coli or the transcriptional repressor of heat-shock genes HrcA in Bacillus subtilis (Hecker et al. (springer.com)
- Actin filaments power cellular movement, bind with hundreds of different cellular components, and serve as tracks for molecular motor proteins. (rockefeller.edu)
- The T4 Gene 32 Protein is intended for molecular biology applications. (qiagen.com)
- A screening technique commonly used in drug discovery can yield important details about the actions of molecular 'glues' in protein interactions. (phys.org)
- Proteins are the key players for virtually all molecular processes within the cell. (phys.org)
- Due to the inherent diversity in the underlying mechanisms, protein-based thermosensors affect different cellular processes such as transcription, translation, protein stability, signal transduction as well as proteolytic processes. (springer.com)
- The alpha/beta fold, which differs from the original chain tracing, shows striking similarity to distinct parts of the signal transduction proteins profilin and the SH2 domain. (embl.de)
- Overall, the high-resolution structure of photoactive yellow protein supports a mechanism whereby electrostatic interactions create an active site poised for photon-induced rearrangements and efficient protein-mediated signal transduction. (embl.de)
- AD is characterized diagnostically by two histologic findings: (1) extracellular amorphus eosinophilic deposits of amyloid consisting of Aβ peptides (a cleavage product of amyloid precursor protein [APP]), which are referred to as amyloid plaques, and (2) intraneuronal aggregates of abnormally modified microtubule-associated protein tau (neurofibrillary tangles) (see the image below). (medscape.com)
- The peptide unit is modeled by trans-N -methylacetamide (NMA) which is allowed to interact with various hydrogen bonding species that are similar to those typically found in the environment of a peptide within a protein molecule. (usu.edu)
- Protein separation conditions always pose the risk of denaturation or structural alteration of the LF molecule. (ift.org)
- 1994). The highly cationic N-terminus region of LF could facilitate charge-induced protein aggregation and inactivate the molecule. (ift.org)
- Inheritance of some variant alleles causes a change in conformation of the alpha-1 antitrypsin molecule, leading to polymerization and retention within hepatocytes. (msdmanuals.com)
- PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). (bvsalud.org)
- The third class of thermosensing is based on the temperature-dependent conformation of specific RNA sequences, which are termed RNA-thermometer (RNAT). (springer.com)
- This binding puts these ssDNA sequences into optimal conformations for interacting with DNA polymerases and other replication proteins. (qiagen.com)
- Fisher C., Ullman O., Stultz CM., Comparative Studies of Disordered Proteins with Similar Sequences: Application to AB40 and AB42. (mit.edu)
- Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. (cdc.gov)
- The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. (bvsalud.org)
- Temperature has a direct effect on fundamental biological systems, including enzyme activity and correct folding of proteins. (springer.com)
- Changes in temperature are typically sensed as a result of conformation changes of protein structure as well as misfolded proteins. (springer.com)
- 6, 7, 8] Alteration in protein conformation with temperature changes also leads to decreased solubility and subsequent vasculitic damage. (medscape.com)
- He shifted his focus from microtubules to actin filaments, another key part of the cytoskeleton made up of long polymers of proteins linked end-to-end. (rockefeller.edu)
- Activated lactoferrin (ALF) is a new form of a naturally occurring protein from milk that acts as a powerful deterrent to pathogenic bacteria that may be present on a meat surface. (ift.org)
- The interaction of LF with microbial surfaces-OMPs of Gram-negative bacteria in particular-has led to other antimicrobial mechanisms, such as the inhibition of microbial attachment to sub-epithelial matrix proteins and detachment of bacteria from mucosal surfaces. (ift.org)
- Many different principles of thermoregulation have been identified in bacteria, which can be assigned to the class of protein-, DNA- or RNA-thermosensors. (springer.com)
- SARS-CoV-2 S protein binds to the ACE2 receptor at the surface of host cells, initially through the S1 RBD. (abcam.com)
- In addition to binding ACE2, increasing evidence suggests that SARS-CoV-2 can also bind other surface proteins to gain cell entry. (abcam.com)
- In a subsequent angiotensin-converting enzyme 2 (ACE2)-spike surrogate neutralization assay, P5C3, and P2G3 exhibited broad and highly potent inhibition of binding (of VOC spike proteins) to ACE2. (news-medical.net)
- Many possess genes that encode proteins to neutralize the affects of antibiotics and prevent attacks on their cell machinery. (icr.org)
- They also intrigued him because they seemed to merge a classical way to think about biology-as a system of genes and proteins-with the lesser understood concept of mechanobiology, "occupying an existential gray area between the microscopic chemical and the macroscopic physical worlds," Alushin says. (rockefeller.edu)
- The shape of things to come: structural insights into how prion proteins encipher heritable information. (cdc.gov)
- The SARS-CoV-2 genome encodes four major structural proteins: the spike (S) protein, nucleocapsid (N) protein, membrane (M) protein and the envelope (E) protein, each of which is essential to compose the viral particle 3 . (abcam.com)
- Proteins are dynamic entities that undergo many structural transitions and fluctuations, which are essential to their biological functions. (europa.eu)
- Hybrid methods that combine computational biophysics with experimental structural biology have proved successful in describing protein conformation, namely their 3D shape. (europa.eu)
- Walker S., Ullman O., Stultz CM. Using Intramolecular Disulfide Bonds in Tau Protein to Deduce Structural Features of Aggregation-resistant Conformations. (mit.edu)
- There are 613402 PAS domains in 396128 proteins in SMART's nrdb database. (embl.de)
- Early in the pandemic, variants of SARS-CoV-2 containing the D614G mutation in the spike (S) protein that increases receptor binding avidity rapidly became dominant in many geographic regions ( 5 , 6 ). (cdc.gov)
- A protein called p63, which is closely related to another protein that suppresses the formation of tumors, plays an essential role in detecting and responding to DNA damage. (elifesciences.org)
- The down state transiently hides the RBD, while the up state exposes the RBD, but temporarily destabilizes the protein subunit 7 , 8 , 9 . (abcam.com)
- Riek R , Hornemann S , Wider G , Billeter M , Glockshuber R , Wüthrich K . NMR structure of the mouse prion protein domain PrP(121-231). (cdc.gov)
- 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. (embl.de)
- The 1.4 A crystallographic structure of photoactive yellow protein, determined by multiple isomorphous replacement methods, provides the first view at atomic resolution of a protein with a photocycle. (embl.de)
- In the dark state structure of photoactive yellow protein, the novel 4-hydroxycinnamyl chromophore, covalently attached to Cys69, is buried within the major hydrophobic core of the protein and is tethered at both ends by hydrogen bonds. (embl.de)
- The T4 Gene 32 Protein has exhibited an ability to enhance the performance of several DNA synthesis-related activities in secondary-structure rich regions, including PCR amplification and DNA sequencing. (qiagen.com)
- Burger V., Nolasco D., Stultz CM., Expanding the Range of Protein Function at the Far end of the Order-Structure Continuum. (mit.edu)
- Linder D., Gurry T., Stultz CM. Towards a Consensus in Protein Structure Nomenclature. (mit.edu)
- Stultz CM. Protein Structure along the order-disorder continuum. (mit.edu)
- The key to understanding proteins-such as those that govern cancer, COVID-19, and other diseases-is quite simple: Identify their chemical structure and find which other proteins can bind to them. (phys.org)
- To test this hypothesis, an occupationally relevant dose of MDI (0.1%w/v) was reacted with varying concentrations of GSH (10µM-10mM), and the reaction products were characterized with regard to mass/structure, and ability to carbamoylate human albumin, a major carrier protein for MDI in vivo. (cdc.gov)
- The TRIP13 gene provides instructions for making a protein that has several roles in cell division. (medlineplus.gov)
- TRIP13 gene mutations involved in MVA syndrome lead to production of an abnormally short protein that is quickly broken down. (medlineplus.gov)
- The native Gene 32 Protein from bacteriophage T4 (T4gp32) is a single-stranded DNA binding protein that is required for T4 DNA replication, recombination and repair. (qiagen.com)
- The T4 Gene 32 Protein also stimulates the rate of synthesis of T4 DNA Polymerase on primed-single-stranded substrates showing a 5-10-fold increase in synthesis rate. (qiagen.com)
- The T4 Gene 32 Protein is a single-stranded nucleic acid binding protein that has the function of stabilizing single-stranded regions of DNA. (qiagen.com)
- The ability of T4 Gene 32 Protein to enhance the performance of several DNA synthesis-related activities is based on its essential function in the replication of bacteriophage T4. (qiagen.com)
- Instructions for using T4 Gene 32 Protein are provided in the corresponding kit protocol in the resources below. (qiagen.com)
- DNA binding of single stranded DNA by T4 Gene 32 Protein was measured using a gel shift assay with a single-stranded, fluorescently labeled oligonucleotide. (qiagen.com)
- Protein concentration (OD 280 ) of T4 Gene 32 Protein was determined by OD 280 absorbance. (qiagen.com)
- Ribosomes, the structures where protein synthesis is catalyzed, are the targets of many other Streptomyces antibiotics such as spectinomycin, tetracycline, and streptomycin. (icr.org)
- Back then, electron microscopy methods to study structures were in their infancy, so one of the things we had to do was to take pictures of proteins using photographic film," he says. (rockefeller.edu)
- He spent many nights alone in a pitch-black lab, utterly silent, utterly still, as he attempted to record protein structures on film, not daring to breathe lest the vibrating air make the image blurry. (rockefeller.edu)
- Dear amber users, I have taken few conformations of a ligand(same ligand)from Protein Data Bank. (vanderbilt.edu)
- These variants carry a constellation of genetic mutations, including in the S protein receptor-binding domain, which is essential for binding to the host cell angiotensin-converting enzyme-2 (ACE-2) receptor to facilitate virus entry. (cdc.gov)
- This protein contains two subunits: the S1 subunit that contains the receptor-binding domain (RBD) and N-terminal domain (NTD), and a second S2 subunit that mediates the fusion of the viral and host cell membranes 4 . (abcam.com)
- The latest VOC, Omicron, carries 37 mutations in its spike protein, most of which lie within the receptor-binding domain (RBD), the target for neutralizing antibodies (nAbs). (news-medical.net)
- While high temperatures account for denatured and misfolded proteins, low temperatures may cause damage to membranes. (springer.com)
- 1991. Isolation and characterization of fatty acid binding protein in the liver of the nurse shark, Ginglymostoma cirratum. (mote.org)
- P2G3 showed the highest binding affinity for the spike protein from ancestral SARS-CoV-2 and a panel of Alpha, Beta, Gamma, and Delta spike proteins . (news-medical.net)
- Improved yields and quality of templates may be achieved with the use of DNA-binding proteins in amplification and sequencing reactions. (qiagen.com)
- The antimicrobial functionality of LF is dependent on its protein conformation and milieu conditions (Naidu and Arnold, 1997). (ift.org)
- A shortage of this protein impairs the spindle assembly checkpoint, and cell division proceeds, even if not all the chromatids are attached to spindle microtubules. (medlineplus.gov)
- Spectinomycin and tetracycline prevent proteins from being assembled by the cell and streptomycin induces the assembly of the wrong amino acids into the translated protein. (icr.org)
- 5,6] Without proteins, which are necessary for normal cell function, the cell dies. (icr.org)
- TMPRSS2 cleavage of the SARS-CoV-2 S protein is believed to enable the fusion of the viral capsid with the host cell to permit viral entry 5 , 6 . (abcam.com)
- Within the trimeric S protein, only one of the three RBD heads is present in the accessible conformation to bind the human Angiotensin 2 (hACE2) host cell receptor 10 . (abcam.com)
- Both Neuropilin-1 and Neuropilin-2 have been shown to bind the cleaved form of the SARS-CoV-2 S protein to mediate host cell entry 13, 14 . (abcam.com)
- 1978. Altered erythrocyte membrane proteins in sickle cell patients associated with the severity of the disease. (mote.org)
- Alushin studies how these little-understood physical dynamics act on the cell's cytoskeleton, an internal network of protein filaments that constantly reconfigures itself to help the cell move, change shape, or ferry molecules from one cell compartment to another. (rockefeller.edu)
- The protein then switches to an active form when DNA damage is detected to trigger the process of cell self-destruction. (elifesciences.org)
- This process is dependent upon activation of the S protein, by cleavage at two sites (S1/S2 and S2') via the proteases Furin and TMPRSS2. (abcam.com)
- Funded by the Marie Skłodowska-Curie Actions programme, the EnLaCES project will present a new hybrid methodology that leverages recent innovations in cryogenic electron microscopy to examine the continuous dynamics and energy landscapes of large, multi-domain proteins. (europa.eu)
- In this proposal, we present a new hybrid methodology that leverages recent innovations in cryo-electron microscopy image analysis to examine continuous dynamics and free energy landscapes of large, multi-domain proteins, which are not achievable with existing methods. (europa.eu)
- Protein dynamics through motions of loops, linkers, and hinges can generate distinctive conformations that are important for protein function. (phys.org)
- Exposure of the RBD in the S1 protein subunit creates an unstable subunit conformation. (abcam.com)
- Cellular stress, or oxidative stress, occurs when there is a buildup of reactive oxygen species (ROS), which interferes with cellular mechanisms and can even cause damage to proteins, lipids, and DNA. (phys.org)
- All species are found to have a restricting influence on the conformation of a peptide bond. (usu.edu)
- Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. (embl.de)
- Taxonomic distribution of proteins containing PAS domain. (embl.de)
- The complete taxonomic breakdown of all proteins with PAS domain is also avaliable . (embl.de)
- Click on the protein counts, or double click on taxonomic names to display all proteins containing PAS domain in the selected taxonomic class. (embl.de)
- One conserved NAC domain was analyzed in all the NAC proteins. (bvsalud.org)
- also found that the oocytes of mice already contain all the proteins necessary to activate p63. (elifesciences.org)
- 4] Failure of DNA to properly separate during these processes results in a bacterium not being able to divide normally or produce functional proteins. (icr.org)
- Upon co-incubation of GSH-MDI reaction products with human albumin, MDI was rapidly transferred to specific lysines of albumin, and the protein's native conformation/charge was altered, based on electrophoretic mobility. (cdc.gov)
- Streptomyces-produced quinolone and coumarin antibiotics, such as novobiocin, interfere with a protein called gyrase that assists in the normal separation of double-stranded DNA during replication of DNA or transcription of messenger RNA. (icr.org)
- Arg52, located in a concavity of the protein surface adjacent to the dominant patch of negative electrostatic potential, shields the chromophore from solvent and is positioned to form a gateway for the phototactic signal. (embl.de)
- The first step in studying a protein's shape was to coax it into forming a crystal-and so many proteins refused to crystallize, making success "a bit too random for my taste," he says. (rockefeller.edu)
- As a result, cells lack TRIP13 protein. (medlineplus.gov)
- Most proteins perform their functions in cells. (phys.org)
- In a study of patients with type II cryoglobulinemia, peripheral blood mononuclear cells from 18 patients were separated into CD3+ (T cells), CD19+ (B cells), and CD14+ (monocytes) and analyzed for the presence of negative-strand HCV RNA and for HCV nonstructural protein 3 (NS3). (medscape.com)
- NS3 protein was also detected in 6 patients: 5 were positive in T cells, 3 in B cells, and 3 in monocytes. (medscape.com)
- Shortly after SARS-CoV emerged at the turn of the 21st century, the spike (S) protein (particularly in its native conformation) was identified as the immunodominant antigen of the virus3. (who.int)
- This means that once the switch to the active form is triggered there is no delay waiting for other proteins to be made, which makes oocytes extremely sensitive to DNA damage. (elifesciences.org)
- Purity was assessed by comparing the aggregate mass of contaminant bands in the concentrated sample to the mass of the protein of interest band in the diluted sample. (qiagen.com)