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  2. Methods to investigate protein–protein interactions - Wikipedia

    en.wikipedia.org/wiki/Methods_to_investigate...

    Whereas the concept of water activity is widely known and utilized in the applied biosciences, its complement—the protein activity which quantitates proteinprotein 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 ...

  3. Protein–protein interaction prediction - Wikipedia

    en.wikipedia.org/wiki/Proteinprotein...

    Proteinprotein 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 proteinprotein interactions is important for the investigation of intracellular signaling pathways, modelling of protein complex ...

  4. Protein–protein interaction - Wikipedia

    en.wikipedia.org/wiki/Proteinprotein_interaction

    Proteinprotein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that ...

  5. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    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.

  6. Cooperative binding - Wikipedia

    en.wikipedia.org/wiki/Cooperative_binding

    The first description of cooperative binding to a multi-site protein was developed by A.V. Hill. [4] Drawing on observations of oxygen binding to hemoglobin and the idea that cooperativity arose from the aggregation of hemoglobin molecules, each one binding one oxygen molecule, Hill suggested a phenomenological equation that has since been named after him:

  7. Allosteric regulation - Wikipedia

    en.wikipedia.org/wiki/Allosteric_regulation

    The two models differ most in their assumptions about subunit interaction and the preexistence of both states. For proteins in which subunits exist in more than two conformations, the allostery landscape model described by Cuendet, Weinstein, and LeVine, [6] can be used. Allosteric regulation may be facilitated by the evolution of large-scale ...

  8. Enzyme induction and inhibition - Wikipedia

    en.wikipedia.org/wiki/Enzyme_induction_and...

    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.

  9. Two-hybrid screening - Wikipedia

    en.wikipedia.org/wiki/Two-hybrid_screening

    Two-hybrid screening (originally known as yeast two-hybrid system or Y2H) is a molecular biology technique used to discover proteinprotein interactions (PPIs) [1] and protein–DNA interactions [2] [3] by testing for physical interactions (such as binding) between two proteins or a single protein and a DNA molecule, respectively.