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34 relations: Active site, Barnase, Barstar, Biomolecular complex, Conformational ensembles, Connexin, Connexon, Electrospray ionization, Enzyme inhibitor, Essential gene, Förster resonance energy transfer, Fuzzy complex, Heterotetramer, Homomeric, Immunoprecipitation, Macromolecular docking, Molecule, Non-covalent interactions, Nuclear magnetic resonance, Peptide, Phosphorylation, Proteasome, Protein, Protein Data Bank, Protein quaternary structure, Protein subunit, Protein–protein interaction, Ribonuclease, RNA polymerase, Saccharomyces cerevisiae, Single particle analysis, Two-hybrid screening, Voltage-gated potassium channel, X-ray crystallography.
Active site
In biology, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction.
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Barnase
Barnase (a portmanteau of "BActerial" "RiboNucleASE") is a bacterial protein that consists of 110 amino acids and has ribonuclease activity.
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Barstar
Barstar is a small protein synthesized by the bacterium Bacillus amyloliquefaciens.
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Biomolecular complex
Biomolecular complex, also called macromolecular complex or biomacromolecular complex, is any biological complex made of more than one molecule of protein, RNA, DNA, lipids, carbohydrates.
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Conformational ensembles
Conformational ensembles, also known as structural ensembles are experimentally constrained computational models describing the structure of intrinsically unstructured proteins.
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Connexin
Connexins (Cx), or gap junction proteins, are structurally related transmembrane proteins that assemble to form vertebrate gap junctions.
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Connexon
In biology, a connexon, also known as a connexin hemichannel, is an assembly of six proteins called connexins that form the pore for a gap junction between the cytoplasm of two adjacent cells.
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Electrospray ionization
Electrospray ionization (ESI) is a technique used in mass spectrometry to produce ions using an electrospray in which a high voltage is applied to a liquid to create an aerosol.
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Enzyme inhibitor
4QI9) An enzyme inhibitor is a molecule that binds to an enzyme and decreases its activity.
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Essential gene
Essential genes are those genes of an organism that are thought to be critical for its survival.
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Förster resonance energy transfer
Förster resonance energy transfer (FRET), fluorescence resonance energy transfer (FRET), resonance energy transfer (RET) or electronic energy transfer (EET) is a mechanism describing energy transfer between two light-sensitive molecules (chromophores).
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Fuzzy complex
Fuzzy complexes are protein complexes, where structural ambiguity or multiplicity exists and is required for biological function.
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Heterotetramer
A heterotetramer is protein containing four non-covalently bound subunits, wherein the subunits are not all identical.
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Homomeric
No description.
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Immunoprecipitation
Immunoprecipitation (IP) is the technique of precipitating a protein antigen out of solution using an antibody that specifically binds to that particular protein.
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Macromolecular docking
Macromolecular docking is the computational modelling of the quaternary structure of complexes formed by two or more interacting biological macromolecules.
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Molecule
A molecule is an electrically neutral group of two or more atoms held together by chemical bonds.
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Non-covalent interactions
A non-covalent interaction differs from a covalent bond in that it does not involve the sharing of electrons, but rather involves more dispersed variations of electromagnetic interactions between molecules or within a molecule.
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Nuclear magnetic resonance
Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a magnetic field absorb and re-emit electromagnetic radiation.
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Peptide
Peptides (from Gr.: πεπτός, peptós "digested"; derived from πέσσειν, péssein "to digest") are short chains of amino acid monomers linked by peptide (amide) bonds.
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Phosphorylation
In chemistry, phosphorylation of a molecule is the attachment of a phosphoryl group.
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Proteasome
Proteasomes are protein complexes which degrade unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds.
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Protein
Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues.
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Protein Data Bank
The Protein Data Bank (PDB) is a crystallographic database for the three-dimensional structural data of large biological molecules, such as proteins and nucleic acids.
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Protein quaternary structure
Protein quaternary structure is the number and arrangement of multiple folded protein subunits in a multi-subunit complex.
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Protein subunit
In structural biology, a protein subunit is a single protein molecule that assembles (or "coassembles") with other protein molecules to form a protein complex.
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Protein–protein interaction
Protein–protein interactions (PPIs) are the physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by electrostatic forces including the hydrophobic effect.
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Ribonuclease
Ribonuclease (commonly abbreviated RNase) is a type of nuclease that catalyzes the degradation of RNA into smaller components.
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RNA polymerase
RNA polymerase (ribonucleic acid polymerase), both abbreviated RNAP or RNApol, official name DNA-directed RNA polymerase, is a member of a family of enzymes that are essential to life: they are found in all organisms (-species) and many viruses.
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Saccharomyces cerevisiae
Saccharomyces cerevisiae is a species of yeast.
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Single particle analysis
Single particle analysis is a group of related computerized image processing techniques used to analyze images from transmission electron microscopy (TEM).
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Two-hybrid screening
Two-hybrid screening (originally known as yeast two-hybrid system or Y2H) is a molecular biology technique used to discover protein–protein interactions (PPIs) and protein–DNA interactions by testing for physical interactions (such as binding) between two proteins or a single protein and a DNA molecule, respectively.
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Voltage-gated potassium channel
Voltage-gated potassium channels (VGKCs) are transmembrane channels specific for potassium and sensitive to voltage changes in the cell's membrane potential.
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X-ray crystallography
X-ray crystallography is a technique used for determining the atomic and molecular structure of a crystal, in which the crystalline atoms cause a beam of incident X-rays to diffract into many specific directions.
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Complex (biochemistry), Complex of proteins, Multi-enzyme complex, Multimeric protein, Multiprotein complex, Oligomeric protein, Protein complexes.
References
[1] https://en.wikipedia.org/wiki/Protein_complex
