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Whereas the concept of water activity is widely known and utilized in the applied biosciences, its complement—the protein activity which quantitates protein–protein interactions—is much less familiar to bioscientists as it is more difficult to determine in dilute solutions of proteins; protein activity is also much harder to determine for ...
Protein–protein interaction prediction is a field combining bioinformatics and structural biology in an attempt to identify and catalog physical interactions between pairs or groups of proteins. Understanding protein–protein interactions is important for the investigation of intracellular signaling pathways, modelling of protein complex ...
The protein protein interactions are displayed in a signed network that describes what type of interactions that are taking place [74] Protein–protein interactions often result in one of the interacting proteins either being 'activated' or 'repressed'. Such effects can be indicated in a PPI network by "signs" (e.g. "activation" or "inhibition").
Enzyme induction is a process in which a molecule (e.g. a drug) induces (i.e. initiates or enhances) the expression of an enzyme. Enzyme inhibition can refer to the inhibition of the expression of the enzyme by another molecule; interference at the enzyme-level, basically with how the enzyme works.
The model is used in a variety of biochemical situations other than enzyme-substrate interaction, including antigen–antibody binding, DNA–DNA hybridization, and protein–protein interaction. [ 17 ] [ 18 ] It can be used to characterize a generic biochemical reaction, in the same way that the Langmuir equation can be used to model generic ...
The favoured model for the enzyme–substrate interaction is the induced fit model. [53] This model proposes that the initial interaction between enzyme and substrate is relatively weak, but that these weak interactions rapidly induce conformational changes in the enzyme that strengthen binding.
Monod-Wyman-Changeux model reaction scheme of a protein made up of two protomers. The protomer can exist under two states, each with a different affinity for the ligand. L is the ratio of states in the absence of ligand, c is the ratio of affinities. Energy diagram of a Monod-Wyman-Changeux model of a protein made up of two protomers.
The group hypothesized that histone proteins modified by acetyl groups added negative charges to the positive lysines, and thus, reduced the interaction between DNA and histones. [15] Histone modification is now considered a major regulatory mechanism that is involved in many different stages of genetic functions. [ 16 ]