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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 ...
Extensions of the model have been proposed for lattices of proteins by various authors. [5] [6] [7] Edelstein argued that the MWC model gave a better account of the data for hemoglobin than the sequential model [3] could do. [8] He and Changeux [9] applied the model to signal transduction. Changeux [10] has discussed the status of the model ...
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.
In molecular biology, an interactome is the whole set of molecular interactions in a particular cell.The term specifically refers to physical interactions among molecules (such as those among proteins, also known as protein–protein interactions, PPIs; or between small molecules and proteins [1]) but can also describe sets of indirect interactions among genes (genetic interactions).
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.
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:
Regulation of gene expression by a hormone receptor Diagram showing at which stages in the DNA-mRNA-protein pathway expression can be controlled. Regulation of gene expression, or gene regulation, [1] includes a wide range of mechanisms that are used by cells to increase or decrease the production of specific gene products (protein or RNA).