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.
In biology, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction.
Barnase (a portmanteau of "BActerial" "RiboNucleASE") is a bacterial protein that consists of 110 amino acids and has ribonuclease activity.
Barstar is a small protein synthesized by the bacterium Bacillus amyloliquefaciens.
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.
Conformational ensembles, also known as structural ensembles are experimentally constrained computational models describing the structure of intrinsically unstructured proteins.
Connexins (Cx), or gap junction proteins, are structurally related transmembrane proteins that assemble to form vertebrate gap junctions.
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.
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.
4QI9) An enzyme inhibitor is a molecule that binds to an enzyme and decreases its activity.
Essential genes are those genes of an organism that are thought to be critical for its survival.
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).
Fuzzy complexes are protein complexes, where structural ambiguity or multiplicity exists and is required for biological function.
A heterotetramer is protein containing four non-covalently bound subunits, wherein the subunits are not all identical.
Immunoprecipitation (IP) is the technique of precipitating a protein antigen out of solution using an antibody that specifically binds to that particular protein.
Macromolecular docking is the computational modelling of the quaternary structure of complexes formed by two or more interacting biological macromolecules.
A molecule is an electrically neutral group of two or more atoms held together by chemical bonds.
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.
Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a magnetic field absorb and re-emit electromagnetic radiation.
Peptides (from Gr.: πεπτός, peptós "digested"; derived from πέσσειν, péssein "to digest") are short chains of amino acid monomers linked by peptide (amide) bonds.
In chemistry, phosphorylation of a molecule is the attachment of a phosphoryl group.
Proteasomes are protein complexes which degrade unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds.
Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues.
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.
Protein quaternary structure is the number and arrangement of multiple folded protein subunits in a multi-subunit complex.
In structural biology, a protein subunit is a single protein molecule that assembles (or "coassembles") with other protein molecules to form a protein complex.
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.
Ribonuclease (commonly abbreviated RNase) is a type of nuclease that catalyzes the degradation of RNA into smaller components.
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.
Saccharomyces cerevisiae is a species of yeast.
Single particle analysis is a group of related computerized image processing techniques used to analyze images from transmission electron microscopy (TEM).
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.
Voltage-gated potassium channels (VGKCs) are transmembrane channels specific for potassium and sensitive to voltage changes in the cell's membrane potential.
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.