A structurally-related family of small proteins that form a stable tertiary fold pattern which is supported by a series of disulfide bonds. The arrangement of disulfide bonds between the CYSTEINE moieties results in a knotted structure which is unique to this family of proteins.
Amino acid sequence in which two disulfide bonds (DISULFIDES) and their connecting backbone form a ring that is penetrated by a third disulfide bond. Members include CYCLOTIDES and agouti-related protein.
A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.
A continuous circle of peptide bonds, typically of 2-3 dozen AMINO ACIDS, so there is no free N- or C-terminus. They are further characterized by six conserved CYSTEINE residues that form CYSTINE KNOT MOTIFS.
A plant family of the order Violales, subclass Dilleniidae, class Magnoliopsida.
A plant genus of the family VIOLACEAE. Some species in this genus are called bouncing bet which is a common name more often used with SAPONARIA OFFICINALIS. Members contain macrocyclic peptides.
Specific assays that measure the migration of cells. They are commonly used to measure the migration of immune cells in response to stimuli and the inhibition of immune cell migration by immunosuppressive factors.
A plant genus of the family RUBIACEAE. Some species are used as an ingredient in Chinese and African traditional medicines. Members contain kalata B1, a macrocyclic peptide.
The Madder plant family of the order Rubiales, subclass Asteridae, class Magnoliopsida includes important medicinal plants that provide QUININE; IPECAC; and COFFEE. They have opposite leaves and interpetiolar stipules.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
A metabolic disease characterized by the defective transport of CYSTINE across the lysosomal membrane due to mutation of a membrane protein cystinosin. This results in cystine accumulation and crystallization in the cells causing widespread tissue damage. In the KIDNEY, nephropathic cystinosis is a common cause of RENAL FANCONI SYNDROME.
Venoms of arthropods of the order Araneida of the ARACHNIDA. The venoms usually contain several protein fractions, including ENZYMES, hemolytic, neurolytic, and other TOXINS, BIOLOGICAL.
The alpha chain of pituitary glycoprotein hormones (THYROTROPIN; FOLLICLE STIMULATING HORMONE; LUTEINIZING HORMONE) and the placental CHORIONIC GONADOTROPIN. Within a species, the alpha subunits of these four hormones are identical; the distinct functional characteristics of these glycoprotein hormones are determined by the unique beta subunits. Both subunits, the non-covalently bound heterodimers, are required for full biologic activity.
Arthropods of the class ARACHNIDA, order Araneae. Except for mites and ticks, spiders constitute the largest order of arachnids, with approximately 37,000 species having been described. The majority of spiders are harmless, although some species can be regarded as moderately harmful since their bites can lead to quite severe local symptoms. (From Barnes, Invertebrate Zoology, 5th ed, p508; Smith, Insects and Other Arthropods of Medical Importance, 1973, pp424-430)
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
'Amino Acid Transport System y+', also known as System Y+, is a sodium-independent cationic amino acid transporter that mediates the uptake of primarily basic amino acids, such as arginine and lysine, into cells through a facilitated diffusion process.
Peptides whose amino and carboxy ends are linked together with a peptide bond forming a circular chain. Some of them are ANTI-INFECTIVE AGENTS. Some of them are biosynthesized non-ribosomally (PEPTIDE BIOSYNTHESIS, NON-RIBOSOMAL).
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
An inherited disorder due to defective reabsorption of CYSTINE and other BASIC AMINO ACIDS by the PROXIMAL RENAL TUBULES. This form of aminoaciduria is characterized by the abnormally high urinary levels of cystine; LYSINE; ARGININE; and ORNITHINE. Mutations involve the amino acid transport protein gene SLC3A1.
A mercaptoethylamine compound that is endogenously derived from the COENZYME A degradative pathway. The fact that cysteamine is readily transported into LYSOSOMES where it reacts with CYSTINE to form cysteine-cysteamine disulfide and CYSTEINE has led to its use in CYSTINE DEPLETING AGENTS for the treatment of CYSTINOSIS.
The process by which two molecules of the same chemical composition form a condensation product or polymer.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
Techniques for securing together the edges of a wound, with loops of thread or similar materials (SUTURES).

Optimizing structural modeling for a specific protein scaffold: knottins or inhibitor cystine knots. (1/14)

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PET imaging of tumor neovascularization in a transgenic mouse model with a novel 64Cu-DOTA-knottin peptide. (2/14)

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Anti-angiogenic effects of two cystine-knot miniproteins from tomato fruit. (3/14)

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Protease-resistant peptide ligands from a knottin scaffold library. (4/14)

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New mode of action for a knottin protein bioinsecticide: pea albumin 1 subunit b (PA1b) is the first peptidic inhibitor of V-ATPase. (5/14)

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Pharmacokinetically stabilized cystine knot peptides that bind alpha-v-beta-6 integrin with single-digit nanomolar affinities for detection of pancreatic cancer. (6/14)

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111In-labeled cystine-knot peptides based on the Agouti-related protein for targeting tumor angiogenesis. (7/14)

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Cyclic peptides arising by evolutionary parallelism via asparaginyl-endopeptidase-mediated biosynthesis. (8/14)

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Cystine-knot miniproteins, also known as "cyclic peptides" or "constrained peptides," are a class of small protein molecules that contain a unique structural motif called a cystine knot. This motif is formed by the presence of three intramolecular disulfide bonds that create a knotted structure, which confers stability and resistance to proteolytic degradation on these miniproteins.

Cystine-knot miniproteins are found in various organisms, including plants, animals, and microorganisms, and have diverse biological functions. Some cystine-knot miniproteins act as toxins or hormones, while others have been shown to have therapeutic potential as drugs or drug delivery agents.

Due to their small size, stability, and specificity, cystine-knot miniproteins are attractive candidates for the development of new drugs and diagnostic tools. They can be engineered to bind to specific targets with high affinity and selectivity, making them useful for a variety of applications in medicine and biotechnology.

Cystine knot motifs are a type of protein structure characterized by the formation of a unique knotted pattern through the linking of three conserved cysteine residues. In this structure, two of the cysteines form a disulfide bond, while the third crosses under and forms an additional disulfide bond with one of the first pair, creating a knot-like shape. This motif is found in a variety of proteins, including some that are involved in important biological processes such as cell signaling, wound healing, and tumor suppression. The cystine knot motif confers stability to these proteins and helps them maintain their function even under harsh conditions.

Cystine is a naturally occurring amino acid in the body, which is formed from the oxidation of two cysteine molecules. It is a non-essential amino acid, meaning that it can be produced by the body and does not need to be obtained through diet. Cystine plays important roles in various biological processes, including protein structure and antioxidant defense. However, when cystine accumulates in large amounts, it can form crystals or stones, leading to conditions such as cystinuria, a genetic disorder characterized by the formation of cystine kidney stones.

Cyclotides are a group of naturally occurring cyclic peptides that contain a head-to-tail cyclized structure and a conserved cystine knot motif. They are produced by plants, particularly those in the Rubiaceae family, as a defense mechanism against herbivores and pathogens.

Cyclotides have unique structural features, including a circular arrangement of amino acids and a knotted pattern of disulfide bonds, which contribute to their stability and resistance to degradation. These properties make them attractive candidates for drug development and therapeutic applications.

In addition to their potential use as drugs, cyclotides have also been studied for their potential as insecticides, antimicrobial agents, and anti-cancer therapies. They have been shown to have potent activity against a variety of targets, including cancer cells, bacteria, fungi, and viruses.

Overall, the unique structural and functional properties of cyclotides make them an exciting area of research in the fields of medicinal chemistry, pharmacology, and drug discovery.

I apologize for any confusion, but "Violaceae" is not a medical term. It is the biological name of a family of flowering plants, also known as the violet family. This family includes various plants that may have medicinal uses, such as violets and pansies, but "Violaceae" itself does not have a specific medical definition.

"Viola" is a term that has different meanings in various scientific and medical contexts. Here are some possible definitions related to medicine and biology:

1. Viola tricolor L. (Heartsease or Johnny-jump-up) - A species of flowering plant in the family Violaceae, which is used in herbal medicine for treating skin conditions, coughs, and respiratory issues.
2. Viola odorata L. (Sweet violet) - Another species of flowering plant in the family Violaceae, whose leaves and flowers are used to make teas, syrups, and other medicinal preparations for treating various ailments such as coughs, colds, and skin conditions.
3. In anatomy, "viola" is an archaic term that refers to the human uvula or the conical piece of soft tissue hanging down at the back of the throat.
4. Viola (musical instrument) - While not directly related to medicine, it's worth noting that "viola" is also a stringed musical instrument similar to a violin but slightly larger and with a deeper sound. In some contexts, such as music therapy, musical instruments can have therapeutic applications in healthcare settings.

It's essential to clarify the specific meaning of "Viola" in the given medical or scientific context since it can refer to different things depending on the field.

Cell migration assays are a type of in vitro laboratory experiments used to study the movement or motility of cells, typically in the context of cellular migration during wound healing, cancer metastasis, inflammation, and embryonic development. These assays allow researchers to quantify and analyze the migratory behavior of various cell types under different experimental conditions.

There are several types of cell migration assays, including:

1. Boyden Chamber Assay: This is a classic and widely used assay that measures the directional migration of cells through a porous membrane towards a chemoattractant source. The cells are placed in the upper chamber, while the chemoattractant is added to the lower chamber. After a set period, the number of cells that have migrated through the membrane to the lower chamber is quantified.
2. Wound Healing Assay: Also known as a scratch assay, this method measures the migration of cells into a wounded area created on a confluent cell monolayer. The width of the wound is measured at different time points, and the rate of wound closure is calculated to determine the migratory capacity of the cells.
3. Transwell Assay: Similar to the Boyden Chamber assay, this method uses a porous membrane in a transwell insert placed in a well of a tissue culture plate. Cells are added to the upper chamber, and a chemoattractant is added to the lower chamber. After incubation, the cells that have migrated through the membrane are stained and quantified.
4. Dunn Chamber Assay: This assay measures the chemotaxis of cells in response to a gradient of chemoattractants. Cells are placed in the center of a circular chamber, and a chemoattractant source is positioned at one end of the chamber. The movement of cells towards the chemoattractant source is recorded and analyzed using time-lapse microscopy.
5. Microfluidic Assay: This assay uses microfabricated channels to create precise gradients of chemoattractants, allowing for the study of cell migration under more physiologically relevant conditions. Cells are introduced into one end of the channel, and their movement towards or away from the chemoattractant gradient is monitored using time-lapse microscopy.

These assays help researchers understand the mechanisms underlying cell migration and can be used to study various aspects of cell behavior, such as chemotaxis, haptotaxis, and durotaxis. Additionally, these assays can be employed to investigate the effects of drugs, genetic modifications, or environmental factors on cell migration, which is crucial for understanding disease progression and developing novel therapeutic strategies.

"Oldenlandia" is not a term that has a specific medical definition. It is a genus of flowering plants in the coffee family, Rubiaceae, and it includes over 200 species that are found primarily in tropical and subtropical regions around the world. Some species of Oldenlandia have been used in traditional medicine in various cultures, but there is limited scientific evidence to support their effectiveness or safety.

In modern medical contexts, if "Oldenlandia" is mentioned, it may refer to a specific plant species that has been studied for its potential medicinal properties. For example, Oldenlandia diffusa (also known as Hedyotis diffusa) has been investigated for its anti-inflammatory, antioxidant, and anticancer effects. However, it is important to note that the use of any plant or herbal remedy should be discussed with a qualified healthcare provider, as they can interact with other medications and have potential side effects.

Rubiaceae is not a medical term, but a taxonomic category in botany. It refers to the family of flowering plants that includes more than 13,500 species, distributed across approximately 600 genera. Some well-known members of this family include coffee (Coffea arabica), gardenias (Gardenia jasminoides), and madder (Rubia tinctorum).

In a medical context, certain plants from the Rubiaceae family have been used in traditional medicine for various purposes. For example:

* Coffee (Coffea arabica) beans are used to prepare caffeinated beverages that can help with alertness and concentration.
* Gardenia fruits and flowers have been used in traditional Chinese medicine to treat anxiety, insomnia, and inflammation.
* Madder root (Rubia tinctorum) has been used as a dye and in traditional medicine to treat skin conditions and digestive disorders.

However, it's important to note that the medicinal use of plants from this family should be based on scientific evidence and under the guidance of healthcare professionals, as some of these plants can have side effects or interact with medications.

Disulfides are a type of organic compound that contains a sulfur-sulfur bond. In the context of biochemistry and medicine, disulfide bonds are often found in proteins, where they play a crucial role in maintaining their three-dimensional structure and function. These bonds form when two sulfhydryl groups (-SH) on cysteine residues within a protein molecule react with each other, releasing a molecule of water and creating a disulfide bond (-S-S-) between the two cysteines. Disulfide bonds can be reduced back to sulfhydryl groups by various reducing agents, which is an important process in many biological reactions. The formation and reduction of disulfide bonds are critical for the proper folding, stability, and activity of many proteins, including those involved in various physiological processes and diseases.

Cystinosis is a rare, inherited metabolic disorder that affects primarily the eyes, kidneys, and liver. It is characterized by an abnormal accumulation of the amino acid cystine within lysosomes (cellular organelles responsible for breaking down and recycling waste products) due to a defect in the gene CTNS that encodes for a protein called cystinosin. This leads to the formation of crystals, which can cause cell damage and multi-organ dysfunction.

There are three main types of cystinosis:

1. Nephropathic or infantile cystinosis: This is the most severe form, with symptoms appearing within the first year of life. It primarily affects the kidneys, leading to Fanconi syndrome (a condition characterized by excessive loss of nutrients in urine), growth failure, and kidney dysfunction. If left untreated, it can progress to end-stage renal disease (ESRD) around the age of 10.
2. Intermediate cystinosis: This form presents during childhood with milder kidney involvement but can still lead to ESRD in adolescence or early adulthood. Eye and central nervous system abnormalities may also be present.
3. Non-nephropathic or ocular cystinosis: This is the mildest form, primarily affecting the eyes. Symptoms include photophobia (sensitivity to light), corneal opacities, and decreased vision. Kidney function remains normal in this type.

Treatment for cystinosis typically involves a combination of medications to manage symptoms and slow disease progression. Cysteamine therapy, which helps remove excess cystine from cells, is the primary treatment for all types of cystinosis. Regular monitoring and management of complications are essential to maintain quality of life and prolong survival.

Spider venoms are complex mixtures of bioactive compounds produced by the specialized glands of spiders. These venoms are primarily used for prey immobilization and defense. They contain a variety of molecules such as neurotoxins, proteases, peptides, and other biologically active substances. Different spider species have unique venom compositions, which can cause different reactions when they bite or come into contact with humans or other animals. Some spider venoms can cause mild symptoms like pain and swelling, while others can lead to more severe reactions such as tissue necrosis or even death in extreme cases.

Glycoprotein hormones are a group of hormones that share a similar structure and are made up of four subunits: two identical alpha subunits and two distinct beta subunits. The alpha subunit is common to all glycoprotein hormones, including thyroid-stimulating hormone (TSH), follicle-stimulating hormone (FSH), luteinizing hormone (LH), and human chorionic gonadotropin (hCG).

The alpha subunit of glycoprotein hormones is a 92 amino acid polypeptide chain that contains several disulfide bonds, which help to stabilize its structure. It is heavily glycosylated, meaning that it contains many carbohydrate groups attached to the protein backbone. The alpha subunit plays an important role in the biological activity of the hormone by interacting with a specific receptor on the target cell surface.

The alpha subunit contains several regions that are important for its function, including a signal peptide, a variable region, and a conserved region. The signal peptide is a short sequence of amino acids at the N-terminus of the protein that directs it to the endoplasmic reticulum for processing and secretion. The variable region contains several amino acid residues that differ between different glycoprotein hormones, while the conserved region contains amino acids that are identical or very similar in all glycoprotein hormones.

Together with the beta subunit, the alpha subunit forms the functional hormone molecule. The beta subunit determines the specificity of the hormone for its target cells and regulates its biological activity.

I'm sorry for any confusion, but "spiders" is not a term that has a specific medical definition. It is a common name used to refer to arachnids of the order Araneae, characterized by having two main body parts (the cephalothorax and abdomen), eight legs, and fangs that inject venom.

However, in a medical context, "spider" or "spider bite" may be used to describe skin lesions or reactions resulting from the bite of certain spiders, particularly those with medically significant venoms. For example, necrotic arachnidism is a condition caused by the bite of some spider species, such as recluse spiders (Loxosceles spp.). The bites can cause skin necrosis and other systemic symptoms in severe cases.

If you are looking for information on a specific medical topic or condition, please provide more details so I can offer a more accurate response.

Cysteine is a semi-essential amino acid, which means that it can be produced by the human body under normal circumstances, but may need to be obtained from external sources in certain conditions such as illness or stress. Its chemical formula is HO2CCH(NH2)CH2SH, and it contains a sulfhydryl group (-SH), which allows it to act as a powerful antioxidant and participate in various cellular processes.

Cysteine plays important roles in protein structure and function, detoxification, and the synthesis of other molecules such as glutathione, taurine, and coenzyme A. It is also involved in wound healing, immune response, and the maintenance of healthy skin, hair, and nails.

Cysteine can be found in a variety of foods, including meat, poultry, fish, dairy products, eggs, legumes, nuts, seeds, and some grains. It is also available as a dietary supplement and can be used in the treatment of various medical conditions such as liver disease, bronchitis, and heavy metal toxicity. However, excessive intake of cysteine may have adverse effects on health, including gastrointestinal disturbances, nausea, vomiting, and headaches.

Protein folding is the process by which a protein molecule naturally folds into its three-dimensional structure, following the synthesis of its amino acid chain. This complex process is determined by the sequence and properties of the amino acids, as well as various environmental factors such as temperature, pH, and the presence of molecular chaperones. The final folded conformation of a protein is crucial for its proper function, as it enables the formation of specific interactions between different parts of the molecule, which in turn define its biological activity. Protein misfolding can lead to various diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

The amino acid transport system y+ is a type of sodium-independent cationic amino acid transporter that is responsible for the uptake of positively charged amino acids, such as arginine and lysine, into cells. It is a part of a larger family of amino acid transporters that are involved in the transport of various types of amino acids across cell membranes.

The y+ system is composed of several different transporter proteins, including rBAT/4F2hc heteromeric amino acid transporter (Cat1), and light chains such as y+LAT1, y+LAT2, and y+LAT3. These transporters are widely expressed in various tissues, including the small intestine, kidney, liver, and brain.

The y+ system plays important roles in various physiological processes, including protein synthesis, immune function, and neurotransmitter metabolism. Dysregulation of this transport system has been implicated in several diseases, such as cancer, neurological disorders, and kidney disease.

Cyclic peptides are a type of peptides in which the N-terminus and C-terminus of the peptide chain are linked to form a circular structure. This is in contrast to linear peptides, which have a straight peptide backbone with a free N-terminus and C-terminus. The cyclization of peptides can occur through various mechanisms, including the formation of an amide bond between the N-terminal amino group and the C-terminal carboxylic acid group (head-to-tail cyclization), or through the formation of a bond between side chain functional groups.

Cyclic peptides have unique structural and chemical properties that make them valuable in medical and therapeutic applications. For example, they are more resistant to degradation by enzymes compared to linear peptides, which can increase their stability and half-life in the body. Additionally, the cyclic structure allows for greater conformational rigidity, which can enhance their binding affinity and specificity to target molecules.

Cyclic peptides have been explored as potential therapeutics for a variety of diseases, including cancer, infectious diseases, and neurological disorders. They have also been used as tools in basic research to study protein-protein interactions and cell signaling pathways.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Secondary protein structure refers to the local spatial arrangement of amino acid chains in a protein, typically described as regular repeating patterns held together by hydrogen bonds. The two most common types of secondary structures are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). In an α-helix, the polypeptide chain twists around itself in a helical shape, with each backbone atom forming a hydrogen bond with the fourth amino acid residue along the chain. This forms a rigid rod-like structure that is resistant to bending or twisting forces. In β-sheets, adjacent segments of the polypeptide chain run parallel or antiparallel to each other and are connected by hydrogen bonds, forming a pleated sheet-like arrangement. These secondary structures provide the foundation for the formation of tertiary and quaternary protein structures, which determine the overall three-dimensional shape and function of the protein.

"Plant proteins" refer to the proteins that are derived from plant sources. These can include proteins from legumes such as beans, lentils, and peas, as well as proteins from grains like wheat, rice, and corn. Other sources of plant proteins include nuts, seeds, and vegetables.

Plant proteins are made up of individual amino acids, which are the building blocks of protein. While animal-based proteins typically contain all of the essential amino acids that the body needs to function properly, many plant-based proteins may be lacking in one or more of these essential amino acids. However, by consuming a variety of plant-based foods throughout the day, it is possible to get all of the essential amino acids that the body needs from plant sources alone.

Plant proteins are often lower in calories and saturated fat than animal proteins, making them a popular choice for those following a vegetarian or vegan diet, as well as those looking to maintain a healthy weight or reduce their risk of chronic diseases such as heart disease and cancer. Additionally, plant proteins have been shown to have a number of health benefits, including improving gut health, reducing inflammation, and supporting muscle growth and repair.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Cystinuria is a genetic disorder that affects the way the body handles certain amino acids, specifically cystine, arginine, lysine, and ornithine. These amino acids are normally reabsorbed in the kidneys and released into the bloodstream. However, people with cystinuria have a defect in the transport mechanism that causes large amounts of cystine to be excreted in the urine, where it can form stones in the urinary tract. These stones can cause pain, blockages, and infection. Cystinuria is inherited in an autosomal recessive manner, meaning that an individual must inherit two copies of the defective gene, one from each parent, to have the condition.

Cysteamine is a medication and a naturally occurring aminothiol compound, which is composed of the amino acid cysteine and a sulfhydryl group. It has various uses in medicine, including as a treatment for cystinosis, a rare genetic disorder that causes an accumulation of cystine crystals in various organs and tissues. Cysteamine works by reacting with cystine to form a compound that can be more easily eliminated from the body. It is available in oral and topical forms and may also be used for other indications, such as treating lung diseases and radiation-induced damage.

Dimerization is a process in which two molecules, usually proteins or similar structures, bind together to form a larger complex. This can occur through various mechanisms, such as the formation of disulfide bonds, hydrogen bonding, or other non-covalent interactions. Dimerization can play important roles in cell signaling, enzyme function, and the regulation of gene expression.

In the context of medical research and therapy, dimerization is often studied in relation to specific proteins that are involved in diseases such as cancer. For example, some drugs have been developed to target and inhibit the dimerization of certain proteins, with the goal of disrupting their function and slowing or stopping the progression of the disease.

Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.

During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.

There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.

Suture techniques refer to the various methods used by surgeons to sew or stitch together tissues in the body after an injury, trauma, or surgical incision. The main goal of suturing is to approximate and hold the edges of the wound together, allowing for proper healing and minimizing scar formation.

There are several types of suture techniques, including:

1. Simple Interrupted Suture: This is one of the most basic suture techniques where the needle is passed through the tissue at a right angle, creating a loop that is then tightened to approximate the wound edges. Multiple stitches are placed along the length of the incision or wound.
2. Continuous Locking Suture: In this technique, the needle is passed continuously through the tissue in a zigzag pattern, with each stitch locking into the previous one. This creates a continuous line of sutures that provides strong tension and support to the wound edges.
3. Running Suture: Similar to the continuous locking suture, this technique involves passing the needle continuously through the tissue in a straight line. However, instead of locking each stitch, the needle is simply passed through the previous loop before being tightened. This creates a smooth and uninterrupted line of sutures that can be easily removed after healing.
4. Horizontal Mattress Suture: In this technique, two parallel stitches are placed horizontally across the wound edges, creating a "mattress" effect that provides additional support and tension to the wound. This is particularly useful in deep or irregularly shaped wounds.
5. Vertical Mattress Suture: Similar to the horizontal mattress suture, this technique involves placing two parallel stitches vertically across the wound edges. This creates a more pronounced "mattress" effect that can help reduce tension and minimize scarring.
6. Subcuticular Suture: In this technique, the needle is passed just below the surface of the skin, creating a smooth and barely visible line of sutures. This is particularly useful in cosmetic surgery or areas where minimizing scarring is important.

The choice of suture technique depends on various factors such as the location and size of the wound, the type of tissue involved, and the patient's individual needs and preferences. Proper suture placement and tension are crucial for optimal healing and aesthetic outcomes.

"Biological Diversity and Therapeutic Potential of Natural and Engineered Cystine Knot Miniproteins." Current Opinion in ... The growth factor cystine knot (GFCK) inhibitor cystine knot (ICK) common in spider and snail toxins Cyclic Cystine Knot, or ... Novel proteins are being added to the cystine knot motif family, also known as the C-terminal cystine knot (CTCK) proteins. ... A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif". Journal of Molecular ...
"Biological Diversity and Therapeutic Potential of Natural and Engineered Cystine Knot Miniproteins." Current Opinion in ... The growth factor cystine knot (GFCK) inhibitor cystine knot (ICK) common in spider and snail toxins Cyclic Cystine Knot, or ... Novel proteins are being added to the cystine knot motif family, also known as the C-terminal cystine knot (CTCK) proteins. ... A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif". Journal of Molecular ...
Cystine-knot miniproteins, also known as knottins, contain a conserved core of three tightly woven disulfide bonds which impart ... Cystine-knot miniproteins, also known as knottins, have shown great potential as molecular scaffolds for the development of ... Cystine-knot miniproteins, also known as knottins, have shown great potential as molecular scaffolds for the development of ... Cystine-knot miniproteins, also known as knottins, constitute a large family of structurally related peptides with diverse ...
Cystine-Knot Miniproteins - Preferred Concept UI. M0539010. Scope note. A structurally-related family of small proteins that ... The arrangement of disulfide bonds between the CYSTEINE moieties results in a knotted structure which is unique to this family ... The arrangement of disulfide bonds between the CYSTEINE moieties results in a knotted structure which is unique to this family ... Miniprotéines à noeud de cystine Entry term(s):. Cystine Knot Miniproteins. Knottin. Knottins. ...
Alternative binding proteins: biological activity and therapeutic potential of cystine-knot miniproteins ... Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: the importance of the cyclic cystine knot ... often grouped with cyclotides as they also contain a cystine knot, but are more closely related to acyclic knottins and are ... which contain an embedded cystine knot of three disulfide bonds that can interact with lipid membranes [32]; cyclic knottins (e ...
Cystine-Knot Miniproteins. *Cytoskeletal Proteins. *Dental Enamel Proteins. *Dietary Proteins. *DNA-Binding Proteins ...
Cystine-Knot Miniproteins [D12.776.217] * Cytoskeletal Proteins [D12.776.220] * Dental Enamel Proteins [D12.776.231] ...
Cystine-Knot Miniproteins. *Diazepam Binding Inhibitor. *Disintegrins. *Distamycins. *Edeine. *Erabutoxins. *Fibrinopeptide A ...
Cystine-Knot Miniproteins. *Cytoskeletal Proteins. *Dental Enamel Proteins. *Dietary Proteins. *DNA-Binding Proteins ...
Launch Cystine-knot peptides, known as knottins frequently, can AT9283 be viewed as as you of Natures combinatorial libraries [ ... Fungus surface-displayed libraries of miniproteins were utilized to choose potent and exclusive matriptase-1 inhibitors. To ... inhibitor cystine-knot) family PP2Bgamma members. Both share the normal architecture of the ICK peptide using the useful loop ... knowledge-based collection design was used that makes usage of complete details on binding and folding behavior of cystine-knot ...
In a knot, there are two cystine molecules connecting different parts of the chain and another in a different direction which ... From the variety of compounds in the venomous liquids, the team found that the most effective products in the tree were "mini proteins ... Another term for this molecular shape is "inhibitor cystine knot" (or aptly ICK or knottin). Apparently, the amino acid chain ... And the cystine is formed from 2 cysteine residues joined end to end through the sulphur atoms (disulphide bond). Cystine is ...
Cystine-Knot Miniproteins [D12.776.217] Cystine-Knot Miniproteins * Cytoskeletal Proteins [D12.776.220] ...
The modelled structure of Df1a, which contains an inhibitor cystine knot motif, is reminiscent of the NaV channel toxin ProTx-I ... These neurotoxins localize specifically to the stinging hairs and are miniproteins of 4 kDa, whose 3D structure is stabilized ... These highly complex and disulfide-rich peptides contain two individual cystine knots, each comprising six cysteines and three ... Structural Conformation and Activity of Spider-Derived Inhibitory Cystine Knot Peptide Pn3a Are Modulated by pH. ...
... that cyclize from head to tail and contain three disulphide bonds to form a complex cystine knot topology.63,64 These molecular ... the linear CVX15 peptide into a cyclotide framework to improve its potency.62 Cyclotides are a special class of globular mini-proteins ... that cyclize from head to tail and contain three disulphide bonds to form a complex cystine knot topology.63,64 These molecular ... that cyclize from head to tail and contain three disulphide bonds to form a complex cystine knot topology.63,64 These molecular ...
Cystine-Knot Miniproteins [D12.776.217] * Cytoskeletal Proteins [D12.776.220] * Dental Enamel Proteins [D12.776.231] ...
Cystine-Knot Miniproteins [D12.776.217] Cystine-Knot Miniproteins * Cytoskeletal Proteins [D12.776.220] ...
Cystine-Knot Miniproteins. *Cytoskeletal Proteins. *Dental Enamel Proteins. *Dietary Proteins. *DNA-Binding Proteins ...
Cystine-Knot Miniproteins. *Cytoskeletal Proteins. *Dental Enamel Proteins. *Dietary Proteins. *DNA-Binding Proteins ...
Cystine-Knot Miniproteins ⌊. Iodoproteins (Iodopeptides) ⌊. Luminescent Proteins (Bioluminescent Proteins) ⌊. Aprotinin ⌊. ...
Cystine-Knot Miniproteins. *Cytoskeletal Proteins. *Dental Enamel Proteins. *Dietary Proteins. *DNA-Binding Proteins ...
Cystine-Knot Miniproteins. *Cytoskeletal Proteins. *Dental Enamel Proteins. *Dietary Proteins. *DNA-Binding Proteins ...
Cystine-Knot Miniproteins ⌊. Iodoproteins (Iodopeptides) ⌊. Luminescent Proteins (Bioluminescent Proteins) ⌊. Aprotinin ⌊. ...
Cystine-Knot Miniproteins. *Cytoskeletal Proteins. *Dental Enamel Proteins. *Dietary Proteins. *DNA-Binding Proteins ...
Cystine-Knot Miniproteins. *Cytoskeletal Proteins. *Dental Enamel Proteins. *Dietary Proteins. *DNA-Binding Proteins ...
Cystine-Knot Miniproteins. *Cytoskeletal Proteins. *Dental Enamel Proteins. *Dietary Proteins. *DNA-Binding Proteins ...
Cystine-Knot Miniproteins. *Cytoskeletal Proteins. *Dental Enamel Proteins. *Dietary Proteins. *DNA-Binding Proteins ...
Cystine-Knot Miniproteins. *Diazepam Binding Inhibitor. *Disintegrins. *Distamycins. *Edeine. *Erabutoxins. *Fibrinopeptide A ...
Cystine-Knot Miniproteins [D12.776.217] * Cytoskeletal Proteins [D12.776.220] * Dental Enamel Proteins [D12.776.231] ...
  • There are three types of cystine knot, which differ in the topology of the disulfide bonds: The growth factor cystine knot (GFCK) inhibitor cystine knot (ICK) common in spider and snail toxins Cyclic Cystine Knot, or cyclotide The growth factor cystine knot was first observed in the structure of nerve growth factor (NGF), solved by X-ray crystallography and published in 1991 by Tom Blundell in Nature. (wikipedia.org)
  • Inhibitor cystine knot (ICK) is a structural motif with a triple stranded antiparallel beta sheet linked by three disulfide bonds, forming a knotted core. (wikipedia.org)
  • Taking into consideration the comprehensive network of hydrogen bonds which permeates the internal core, the (MCoTI especially, Amount 1A) as well as the squirting cucumber (EETI) are prominent associates from the ICK (inhibitor cystine-knot) family PP2Bgamma members. (vaggi.org)
  • This conformational exchange is especially peculiar for peptides containing an inhibitor cystine knot motif, which confers excellent structural stability under conditions that are not conducive to disulfide shuffling. (bvsalud.org)
  • Launch Cystine-knot peptides, known as knottins frequently, can AT9283 be viewed as as you of Natures combinatorial libraries [1]C[4]. (vaggi.org)
  • To this final end, a knowledge-based collection design was used that makes usage of complete details on binding and folding behavior of cystine-knot peptides. (vaggi.org)
  • On the other hand, lately reported miniproteins isolated from spinach (SOTI ICIII, Amount 1B) show no similarity to known place protease inhibitors, but to antimicrobial peptides in the seeds of using the inhibitory loop located between CysV AT9283 and CysVI (Amount 1) [12], [13]. (vaggi.org)
  • A cystine knot is a protein structural motif containing three disulfide bridges (formed from pairs of cysteine residues). (wikipedia.org)
  • The cystine knot motif stabilizes protein structure and is conserved in proteins across various species. (wikipedia.org)
  • These are structurally related due to the presence of the cystine knot motif but differ in sequence. (wikipedia.org)
  • The presence of the cyclic cystine knot (CCK) motif was discovered when cyclotides were isolated from various plant families. (wikipedia.org)
  • The CCK motif has a cyclic backbone, triple stranded beta sheet, and cystine knot conformation. (wikipedia.org)
  • Novel proteins are being added to the cystine knot motif family, also known as the C-terminal cystine knot (CTCK) proteins. (wikipedia.org)
  • The stability and structure of the cystine knot motif implicates possible applications in drug design. (wikipedia.org)
  • Studies have shown that cystine knot proteins can be incubated at temperatures of 65 °C or placed in 1N HCl/1N NaOH without loss of structural and functional integrity. (wikipedia.org)
  • The arrangement of disulfide bonds between the CYSTEINE moieties results in a knotted structure which is unique to this family of proteins. (bvsalud.org)
  • Three -strands connected through three disulfide bonds define their structural primary, where in fact the ring-forming connection of CysI to CysIV and CysII to CysV is normally penetrated with a third cystine between CysIII and CysVI (Amount 1) [1]C[4]. (vaggi.org)
  • There are three types of cystine knot, which differ in the topology of the disulfide bonds: The growth factor cystine knot (GFCK) inhibitor cystine knot (ICK) common in spider and snail toxins Cyclic Cystine Knot, or cyclotide The growth factor cystine knot was first observed in the structure of nerve growth factor (NGF), solved by X-ray crystallography and published in 1991 by Tom Blundell in Nature. (wikipedia.org)
  • The presence of the cyclic cystine knot (CCK) motif was discovered when cyclotides were isolated from various plant families. (wikipedia.org)
  • 1. Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: the importance of the cyclic cystine knot. (nih.gov)
  • 8. Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. (nih.gov)
  • The CCK motif has a cyclic backbone, triple stranded beta sheet, and cystine knot conformation. (wikipedia.org)
  • A cystine knot is a protein structural motif containing three disulfide bridges (formed from pairs of cysteine residues). (wikipedia.org)
  • Inhibitor cystine knot (ICK) is a structural motif with a triple stranded antiparallel beta sheet linked by three disulfide bonds, forming a knotted core. (wikipedia.org)
  • 19. Solution structure by NMR of circulin A: a macrocyclic knotted peptide having anti-HIV activity. (nih.gov)
  • 5. The cyclotide family of circular miniproteins: nature's combinatorial peptide template. (nih.gov)
  • Tying the knot within the circular backbone of the cyclotides. (nih.gov)
  • The stability and structure of the cystine knot motif implicates possible applications in drug design. (wikipedia.org)
  • Characterization of cystine knot and beta-sheet formation in the macrocyclic polypeptide kalata B1. (nih.gov)
  • 6. Chemical synthesis and folding pathways of large cyclic polypeptides: studies of the cystine knot polypeptide kalata B1. (nih.gov)