An order of anaerobic methanogens in the kingdom EURYARCHAEOTA. They are pseudosarcina, coccoid or sheathed rod-shaped and catabolize methyl groups. The cell wall is composed of protein. The order includes one family, METHANOCOCCACEAE. (From Bergey's Manual of Systemic Bacteriology, 1989)
A family of anaerobic METHANOCOCCALES whose organisms are motile by means of flagella. These methanogens use carbon dioxide as an electron acceptor.
A genus of obligate anaerobic METHANOCALDOCOCCACEAE whose organisms are non-motile despite possessing long thin flagella. These methanogens are found in deep-sea vent and other hydrothermal environments.
Proteins found in any species of archaeon.
A genus of anaerobic coccoid METHANOCOCCACEAE whose organisms are motile by means of polar tufts of flagella. These methanogens are found in salt marshes, marine and estuarine sediments, and the intestinal tract of animals.
Ribonucleic acid in archaea having regulatory and catalytic roles as well as involvement in protein synthesis.
The functional genetic units of ARCHAEA.
A transfer RNA which is specific for carrying cysteine to sites on the ribosomes in preparation for protein synthesis.
Catalyze the hydrolysis of nucleotides with the elimination of ammonia.
Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in archaea.
Ribose substituted in the 1-, 3-, or 5-position by a phosphoric acid moiety.
The processes by which organisms use simple inorganic substances such as gaseous or dissolved carbon dioxide and inorganic nitrogen as nutrient sources. Contrasts with heterotrophic processes which make use of organic materials as the nutrient supply source. Autotrophs can be either chemoautotrophs (or chemolithotrophs), largely ARCHAEA and BACTERIA, which also use simple inorganic substances for their metabolic energy reguirements; or photoautotrophs (or photolithotrophs), such as PLANTS and CYANOBACTERIA, which derive their energy from light. Depending on environmental conditions some organisms can switch between different nutritional modes (autotrophy; HETEROTROPHY; chemotrophy; or PHOTOTROPHY) to utilize different sources to meet their nutrient and energy requirements.
Deoxyribonucleic acid that makes up the genetic material of archaea.
One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.
A family of anaerobic, coccoid to rod-shaped METHANOBACTERIALES. Cell membranes are composed mainly of polyisoprenoid hydrocarbons ether-linked to glycerol. Its organisms are found in anaerobic habitats throughout nature.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The simplest saturated hydrocarbon. It is a colorless, flammable gas, slightly soluble in water. It is one of the chief constituents of natural gas and is formed in the decomposition of organic matter. (Grant & Hackh's Chemical Dictionary, 5th ed)
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.
A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
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.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.
The relationships of groups of organisms as reflected by their genetic makeup.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
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).
Proteins prepared by recombinant DNA technology.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

Crystal structure of putative CbiT from Methanocaldococcus jannaschii: an intermediate enzyme activity in cobalamin (vitamin B12) biosynthesis. (1/7)

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Crucial optimization of translational components towards efficient incorporation of unnatural amino acids into proteins in mammalian cells. (2/7)

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Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei. (3/7)

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Structure of the SecY channel during initiation of protein translocation. (4/7)

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Identification of a 5'-deoxyadenosine deaminase in Methanocaldococcus jannaschii and its possible role in recycling the radical S-adenosylmethionine enzyme reaction product 5'-deoxyadenosine. (5/7)

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Thioredoxin targets fundamental processes in a methane-producing archaeon, Methanocaldococcus jannaschii. (6/7)

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Keeping it simple, transport mechanism and pH regulation in Na+/H+ exchangers. (7/7)

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Methanococcales is an order of methanogenic archaea within the kingdom Euryarchaeota. These are microorganisms that produce methane as a metabolic byproduct in anaerobic environments. Members of this order are distinguished by their ability to generate energy through the reduction of carbon dioxide with hydrogen gas, a process known as CO2 reduction. They are typically found in marine sediments, deep-sea vents, and other extreme habitats. The most well-known genus within Methanococcales is Methanococcus, which includes several species that are capable of living at relatively high temperatures and pressures.

Methanococcaceae is a family of archaea within the order Methanococcales. These are obligate anaerobic, methanogenic microorganisms that are commonly found in marine and freshwater environments. They can also be found in association with animals, including humans, where they may play a role in digestion. Members of this family are characterized by their ability to produce methane as a metabolic end-product using hydrogen and carbon dioxide as substrates. Some notable genera within this family include Methanococcus, Methanothermococcus, and Methanocaldococcus.

I'm sorry for any confusion, but "Methanocaldococcus" is not a medical term. It is a genus of methanogenic archaea that are capable of producing methane at relatively high temperatures, typically above 65 degrees Celsius. These organisms are often found in hydrothermal vents and other extreme environments. They are not directly related to human health or medicine.

Archaeal proteins are proteins that are encoded by the genes found in archaea, a domain of single-celled microorganisms. These proteins are crucial for various cellular functions and structures in archaea, which are adapted to survive in extreme environments such as high temperatures, high salt concentrations, and low pH levels.

Archaeal proteins share similarities with both bacterial and eukaryotic proteins, but they also have unique features that distinguish them from each other. For example, many archaeal proteins contain unusual amino acids or modifications that are not commonly found in other organisms. Additionally, the three-dimensional structures of some archaeal proteins are distinct from their bacterial and eukaryotic counterparts.

Studying archaeal proteins is important for understanding the biology of these unique organisms and for gaining insights into the evolution of life on Earth. Furthermore, because some archaea can survive in extreme environments, their proteins may have properties that make them useful in industrial and medical applications.

"Methanococcus" is a genus of archaea, which are single-celled microorganisms that share some characteristics with bacteria but are actually more closely related to eukaryotes. "Methanococcus" species are obligate anaerobes, meaning they can only survive in environments without oxygen. They are also methanogens, which means they produce methane as a byproduct of their metabolism. These microorganisms are commonly found in aquatic environments such as marine sediments and freshwater swamps, where they play an important role in the carbon cycle by breaking down organic matter and producing methane. Some "Methanococcus" species can also be found in the digestive tracts of animals, including humans, where they help to break down food waste and produce methane as a byproduct.

Archaeal RNA refers to the Ribonucleic acid (RNA) molecules that are present in archaea, which are a domain of single-celled microorganisms. RNA is a nucleic acid that plays a crucial role in various biological processes, such as protein synthesis, gene expression, and regulation of cellular activities.

Archaeal RNAs can be categorized into different types based on their functions, including:

1. Messenger RNA (mRNA): It carries genetic information from DNA to the ribosome, where it is translated into proteins.
2. Transfer RNA (tRNA): It helps in translating the genetic code present in mRNA into specific amino acids during protein synthesis.
3. Ribosomal RNA (rRNA): It is a structural and functional component of ribosomes, where protein synthesis occurs.
4. Non-coding RNA: These are RNAs that do not code for proteins but have regulatory functions in gene expression and other cellular processes.

Archaeal RNAs share similarities with both bacterial and eukaryotic RNAs, but they also possess unique features that distinguish them from the other two domains of life. For example, archaeal rRNAs contain unique sequence motifs and secondary structures that are not found in bacteria or eukaryotes. These differences suggest that archaeal RNAs have evolved to adapt to the extreme environments where many archaea live.

Overall, understanding the structure, function, and evolution of archaeal RNA is essential for gaining insights into the biology of these unique microorganisms and their roles in various cellular processes.

I'm happy to help! However, I believe there might be a slight mistake in your question. "Archaeal" is not a term used to describe genes but rather a group of single-celled organisms that are classified as archaea.

Archaea are one of the three domains of life, along with bacteria and eukaryotes (which include plants, animals, and fungi). Archaea are unique because they share characteristics with both bacteria and eukaryotes, but they also have many features that are distinctly their own. For example, archaea have a different cell membrane structure than bacteria and eukaryotes, which allows them to thrive in extreme environments such as hot springs, salt mines, and deep-sea vents.

Genes, on the other hand, are segments of DNA that contain the instructions for making proteins or performing other important functions in an organism's cells. All living organisms, including archaea, have genes that are passed down from generation to generation. Archaeal genes are made up of the same four nucleotides (A, T, C, and G) as bacterial and eukaryotic genes, and they code for proteins and RNA molecules that are essential for the survival and reproduction of archaea.

So, to summarize, there is no specific definition for "Archaeal genes" because "archaeal" is not a term used to describe genes. However, we can say that archaeal genes are segments of DNA that contain the instructions for making proteins and performing other important functions in archaea.

Transfer RNA (tRNA) that carries the amino acid cysteine (Cys) is a type of adaptor molecule in the process of translation during protein synthesis. The genetic code for cysteine is UGU and UGC, which are the anticodon sequences on specific tRNAs. These tRNA molecules recognize and bind to the corresponding mRNA codons through base-pairing, allowing for the addition of cysteine to the growing polypeptide chain in a ribosome. The tRNA^Cys plays a crucial role in maintaining the fidelity and efficiency of protein synthesis.

Nucleotide deaminases are a group of enzymes that catalyze the removal of an amino group (-NH2) from nucleotides, which are the building blocks of DNA and RNA. Specifically, these enzymes convert cytidine or adenosine to uridine or inosine, respectively, by removing an amino group from the corresponding nitrogenous base (cytosine or adenine).

There are several types of nucleotide deaminases that differ in their substrate specificity and cellular localization. For example, some enzymes deaminate DNA or RNA directly, while others act on free nucleotides or nucleosides. Nucleotide deaminases play important roles in various biological processes, including the regulation of gene expression, immune response, and DNA repair.

Abnormal activity or mutations in nucleotide deaminases have been associated with several human diseases, such as cancer, autoimmune disorders, and viral infections. Therefore, understanding the function and regulation of these enzymes is crucial for developing new therapeutic strategies to treat these conditions.

Gene expression regulation in archaea refers to the complex cellular processes that control the transcription and translation of genes into functional proteins. This regulation is crucial for the survival and adaptation of archaea to various environmental conditions.

Archaea, like bacteria and eukaryotes, use a variety of mechanisms to regulate gene expression, including:

1. Transcriptional regulation: This involves controlling the initiation, elongation, and termination of transcription by RNA polymerase. Archaea have a unique transcription machinery that is more similar to eukaryotic RNA polymerases than bacterial ones. Transcriptional regulators, such as activators and repressors, bind to specific DNA sequences near the promoter region to modulate transcription.
2. Post-transcriptional regulation: This includes processes like RNA processing, modification, and degradation that affect mRNA stability and translation efficiency. Archaea have a variety of RNA-binding proteins and small non-coding RNAs (sRNAs) that play crucial roles in post-transcriptional regulation.
3. Translational regulation: This involves controlling the initiation, elongation, and termination of translation by ribosomes. Archaea use a unique set of translation initiation factors and tRNA modifications to regulate protein synthesis.
4. Post-translational regulation: This includes processes like protein folding, modification, and degradation that affect protein stability and function. Archaea have various chaperones, proteases, and modifying enzymes that participate in post-translational regulation.

Overall, gene expression regulation in archaea is a highly dynamic and coordinated process involving multiple layers of control to ensure proper gene expression under changing environmental conditions.

Ribose monophosphates are organic compounds that play a crucial role in the metabolism of cells, particularly in energy transfer and nucleic acid synthesis. A ribose monophosphate is formed by the attachment of a phosphate group to a ribose molecule, which is a type of sugar known as a pentose.

In biochemistry, there are two important ribose monophosphates:

1. Alpha-D-Ribose 5-Phosphate (ADP-Ribose): This compound serves as an essential substrate in various cellular processes, including DNA repair, chromatin remodeling, and protein modification. The enzyme that catalyzes the formation of ADP-ribose is known as poly(ADP-ribose) polymerase (PARP).
2. Ribulose 5-Phosphate: This compound is a key intermediate in the Calvin cycle, which is the process by which plants and some bacteria convert carbon dioxide into glucose during photosynthesis. Ribulose 5-phosphate is formed from ribose 5-phosphate through a series of enzymatic reactions.

Ribose monophosphates are essential for the proper functioning of cells and have implications in various physiological processes, as well as in certain disease states.

Autotrophic processes refer to the ability of certain organisms, known as autotrophs, to synthesize their own organic nutrients from inorganic substances using light or chemical energy. This process is essential for the production of organic matter and the formation of the basis of food chains in ecosystems.

In autotrophic processes, organisms use energy to convert carbon dioxide into organic compounds, such as glucose, through a series of metabolic reactions known as carbon fixation. There are two main types of autotrophic processes: photosynthesis and chemosynthesis.

Photosynthesis is the process used by plants, algae, and some bacteria to convert light energy from the sun into chemical energy in the form of organic compounds. This process involves the use of chlorophyll and other pigments to capture light energy, which is then converted into ATP and NADPH through a series of reactions known as the light-dependent reactions. These energy carriers are then used to power the Calvin cycle, where carbon dioxide is fixed into organic compounds.

Chemosynthesis, on the other hand, is the process used by some bacteria to convert chemical energy from inorganic substances, such as hydrogen sulfide or methane, into organic compounds. This process does not require light energy and typically occurs in environments with limited access to sunlight, such as deep-sea vents or soil.

Overall, autotrophic processes are critical for the functioning of ecosystems and the production of food for both plants and animals.

Archaeal DNA refers to the genetic material present in archaea, a domain of single-celled microorganisms lacking a nucleus. Like bacteria, archaea have a single circular chromosome that contains their genetic information. However, archaeal DNA is significantly different from bacterial and eukaryotic DNA in terms of its structure and composition.

Archaeal DNA is characterized by the presence of unique modifications such as methylation patterns, which help distinguish it from other types of DNA. Additionally, archaea have a distinct set of genes involved in DNA replication, repair, and recombination, many of which are more similar to those found in eukaryotes than bacteria.

One notable feature of archaeal DNA is its resistance to environmental stressors such as extreme temperatures, pH levels, and salt concentrations. This allows archaea to thrive in some of the most inhospitable environments on Earth, including hydrothermal vents, acidic hot springs, and highly saline lakes.

Overall, the study of archaeal DNA has provided valuable insights into the evolutionary history of life on Earth and the unique adaptations that allow these organisms to survive in extreme conditions.

Archaea are a domain of single-celled microorganisms that lack membrane-bound nuclei and other organelles. They are characterized by the unique structure of their cell walls, membranes, and ribosomes. Archaea were originally classified as bacteria, but they differ from bacteria in several key ways, including their genetic material and metabolic processes.

Archaea can be found in a wide range of environments, including some of the most extreme habitats on Earth, such as hot springs, deep-sea vents, and highly saline lakes. Some species of Archaea are able to survive in the absence of oxygen, while others require oxygen to live.

Archaea play important roles in global nutrient cycles, including the nitrogen cycle and the carbon cycle. They are also being studied for their potential role in industrial processes, such as the production of biofuels and the treatment of wastewater.

Methanobacteriaceae is a family of archaea within the order Methanobacteriales. These are obligate anaerobes that obtain energy for growth by reducing carbon dioxide to methane, a process called methanogenesis. They are commonly found in anaerobic environments such as wetlands, digestive tracts of animals, and sewage sludge. Some species are thermophilic, meaning they prefer higher temperatures, while others are mesophilic, growing best at moderate temperatures. Methanobacteriaceae are important contributors to the global carbon cycle and have potential applications in bioremediation and bioenergy production.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

Methane is not a medical term, but it is a chemical compound that is often mentioned in the context of medicine and health. Medically, methane is significant because it is one of the gases produced by anaerobic microorganisms during the breakdown of organic matter in the gut, leading to conditions such as bloating, cramping, and diarrhea. Excessive production of methane can also be a symptom of certain digestive disorders like irritable bowel syndrome (IBS) and small intestinal bacterial overgrowth (SIBO).

In broader terms, methane is a colorless, odorless gas that is the primary component of natural gas. It is produced naturally by the decomposition of organic matter in anaerobic conditions, such as in landfills, wetlands, and the digestive tracts of animals like cows and humans. Methane is also a potent greenhouse gas with a global warming potential 25 times greater than carbon dioxide over a 100-year time frame.

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.

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) are a group of enzymes that play a crucial role in protein synthesis. They are responsible for attaching specific amino acids to their corresponding transfer RNAs (tRNAs), creating aminoacyl-tRNA complexes. These complexes are then used in the translation process to construct proteins according to the genetic code.

Each aminoacyl-tRNA synthetase is specific to a particular amino acid, and there are 20 different synthetases in total, one for each of the standard amino acids. The enzymes catalyze the reaction between an amino acid and ATP to form an aminoacyl-AMP intermediate, which then reacts with the appropriate tRNA to create the aminoacyl-tRNA complex. This two-step process ensures the fidelity of the translation process by preventing mismatching of amino acids with their corresponding tRNAs.

Defects in aminoacyl-tRNA synthetases can lead to various genetic disorders and diseases, such as Charcot-Marie-Tooth disease type 2D, distal spinal muscular atrophy, and leukoencephalopathy with brainstem and spinal cord involvement and lactate acidosis (LBSL).

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.

A protein subunit refers to a distinct and independently folding polypeptide chain that makes up a larger protein complex. Proteins are often composed of multiple subunits, which can be identical or different, that come together to form the functional unit of the protein. These subunits can interact with each other through non-covalent interactions such as hydrogen bonds, ionic bonds, and van der Waals forces, as well as covalent bonds like disulfide bridges. The arrangement and interaction of these subunits contribute to the overall structure and function of the protein.

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.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Crystallization is a process in which a substance transitions from a liquid or dissolved state to a solid state, forming a crystal lattice. In the medical context, crystallization can refer to the formation of crystals within the body, which can occur under certain conditions such as changes in pH, temperature, or concentration of solutes. These crystals can deposit in various tissues and organs, leading to the formation of crystal-induced diseases or disorders.

For example, in patients with gout, uric acid crystals can accumulate in joints, causing inflammation, pain, and swelling. Similarly, in nephrolithiasis (kidney stones), minerals in the urine can crystallize and form stones that can obstruct the urinary tract. Crystallization can also occur in other medical contexts, such as in the formation of dental calculus or plaque, and in the development of cataracts in the eye.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

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.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis, the process by which cells create proteins. In protein synthesis, tRNAs serve as adaptors, translating the genetic code present in messenger RNA (mRNA) into the corresponding amino acids required to build a protein.

Each tRNA molecule has a distinct structure, consisting of approximately 70-90 nucleotides arranged in a cloverleaf shape with several loops and stems. The most important feature of a tRNA is its anticodon, a sequence of three nucleotides located in one of the loops. This anticodon base-pairs with a complementary codon on the mRNA during translation, ensuring that the correct amino acid is added to the growing polypeptide chain.

Before tRNAs can participate in protein synthesis, they must be charged with their specific amino acids through an enzymatic process involving aminoacyl-tRNA synthetases. These enzymes recognize and bind to both the tRNA and its corresponding amino acid, forming a covalent bond between them. Once charged, the aminoacyl-tRNA complex is ready to engage in translation and contribute to protein formation.

In summary, transfer RNA (tRNA) is a small RNA molecule that facilitates protein synthesis by translating genetic information from messenger RNA into specific amino acids, ultimately leading to the creation of functional proteins within cells.

Phylogeny is the evolutionary history and relationship among biological entities, such as species or genes, based on their shared characteristics. In other words, it refers to the branching pattern of evolution that shows how various organisms have descended from a common ancestor over time. Phylogenetic analysis involves constructing a tree-like diagram called a phylogenetic tree, which depicts the inferred evolutionary relationships among organisms or genes based on molecular sequence data or other types of characters. This information is crucial for understanding the diversity and distribution of life on Earth, as well as for studying the emergence and spread of diseases.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

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.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

ISBN 978-0-387-98771-2. PubMed references for Methanocaldococcus PubMed Central references for Methanocaldococcus Google ... for Methanocaldococcus NCBI taxonomy page for Methanocaldococcus Search Tree of Life taxonomy pages for Methanocaldococcus ... Search Species2000 page for Methanocaldococcus MicrobeWiki page for Methanocaldococcus LPSN page for Methanocaldococcus ... List of Archaea genera Methanocaldococcus sp. FS406-22 See the NCBI webpage on Methanocaldococcus. Data extracted from the " ...
Methanocaldococcus jannaschii DSM 2661). Find diseases associated with this biological target and compounds tested against it ...
SOLUTION STRUCTURE OF PUTATIVE UNCHARACTERIZED PROTEIN GSU1278 FROM METHANOCALDOCOCCUS JANNASCHII, NORTHEAST STRUCTURAL ... SOLUTION STRUCTURE OF PUTATIVE UNCHARACTERIZED PROTEIN GSU1278 FROM METHANOCALDOCOCCUS JANNASCHII, NORTHEAST STRUCTURAL ... SOLUTION STRUCTURE OF PUTATIVE UNCHARACTERIZED PROTEIN GSU1278 FROM METHANOCALDOCOCCUS JANNASCHII, NORTHEAST STRUCTURAL ...
Methanocaldococcus jannaschii 1hv8_a Q58083 99.30 7.50E-17 9.10E-21 173.80 0 0 0 0 0 0 0 0 ...
Find proteins for Q57840 (Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)) ... Find proteins for Q60351 (Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)) ...
FROM METHANOCALDOCOCCUS JANNASCHII. NORTHEAST STRUCTURAL GENOMICS TARGET MJR118E - 3DM3 , canSARS ... CRYSTAL STRUCTURE OF A DOMAIN OF A REPLICATION FACTOR A PROTEIN, FROM METHANOCALDOCOCCUS JANNASCHII. NORTHEAST STRUCTURAL ... CRYSTAL STRUCTURE OF A DOMAIN OF A REPLICATION FACTOR A PROTEIN, FROM METHANOCALDOCOCCUS JANNASCHII. NORTHEAST STRUCTURAL ...
Hmdii From Methanocaldococcus Jannaschii Reconstitued with Fe- Guanylylpyridinol (Fegp) Cofactor and Co-Crystallized with ... The structure of Hmdii From Methanocaldococcus Jannaschii Reconstitued with Fe- Guanylylpyridinol (Fegp) Cofactor and Co- ... A full contact list of Iron with other atoms in the Fe binding site number 1 of Hmdii From Methanocaldococcus Jannaschii ... In total only one binding site of Iron was determined in the Hmdii From Methanocaldococcus Jannaschii Reconstitued with Fe- ...
Crystal Structure of L30e a ribosomal protein from Methanocaldococcus jannaschii DSM2661 (MJ1044) ... Crystal Structure of L30e a ribosomal protein from Methanocaldococcus jannaschii DSM2661 (MJ1044); X-RAY DIFFRACTION 1.90 Å ...
Grochowski LL, Xu H, White RH (May 2006). "Methanocaldococcus jannaschii uses a modified mevalonate pathway for biosynthesis of ...
Methanocaldococcus jannaschii (2). *. Mirabilis jalapa (1). *. Mus musculus (14). *. Nicotiana benthamiana (1). ...
Methanocaldococcus jannaschii DSM 2661. Protein translocase subunit SecY. PDB Structure. PDB. 1RH5 ...
Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in Methanocaldococcus jannaschii. J. Bacteriol. 189, 4391- ...
Species Methanocaldococcus jannaschii [TaxId:2190] [189266] (1 PDB entry). *. Domain d3lpef_: 3lpe F: [180497]. automated match ... d3lpef_ g.41.9.0 (F:) automated matches {Methanocaldococcus jannaschii [TaxId: 2190]} ...
Crystal Structure of Succinyl-CoA Synthetase Alpha Chain from Methanocaldococcus jannaschii DSM 2661. ...
The enzyme, which was isolated from the archaeon Methanocaldococcus jannaschii, plays a key role in an alternative pathway for ... semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus ...
... conventional amber and ochre stop codons can be separately targeted by engineered amber-suppressing Methanocaldococcus ... conventional amber and ochre stop codons can be separately targeted by engineered amber-suppressing Methanocaldococcus ...
The enzyme, isolated from the archaeon Methanocaldococcus jannaschii, is involved in sulfite detoxification and assimilation.. ... from the methanarchaeon Methanocaldococcus jannaschii. J. Biol. Chem. 280 (2005) 38776-38786. [DOI] [PMID: 16048999] ...
Recombinant Methanocaldococcus jannaschii Uncharacterized protein MJ0645(MJ0645). CSB-CF688221MRU. in vitro E.coli expression ... Recombinant Methanocaldococcus jannaschii Putative zinc metalloprotease MJ0611(MJ0611). CSB-CF682236MRU. in vitro E.coli ...
The enzyme, isolated from the archaeon Methanocaldococcus jannaschii, participates in the biosynthesis of the methanofuran ...
Methanocaldococcus janaschii1-3 and Archaeoglobus fulgidus, both TyrRS systems), the addition of a third OTS to this group is ... Diese stammen von Methanocaldococcus janaschii1-3 und Archaeoglobus fulgidus (beides TyrRS Systeme). Ein drittes OTS in dieser ... Methanocaldococcus janaschii1-3 and Archaeoglobus fulgidus, both TyrRS systems), the addition of a third OTS to this group is ...
... pEXT9a-like plasmids were found to be closely related to the previously sequenced plasmid pMETVU01 from Methanocaldococcus ...
Methanocaldococcus sp. FS406-22 chromosome, complete genome. DEAD/DEAH box helicase domain protein. 7e-07. 57. ...
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