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Allostery Inhibitors

One of the most important mechanisms for regulating protein function entails allostery. Broadly speaking, allostery refers to any change in a protein s tertiary or quaternary structure or both induced by the binding of a ligand, which may be an activator, inhibitor, substrate, or all three. Allosteric regulation is particularly prevalent in multlmerlc enzymes and other proteins. We first explore several ways in which allostery influences protein function and then consider other mechanisms for regulating proteins. [Pg.83]

In allostery, the binding of one ligand molecule (a substrate, activator, or inhibitor) Induces a conformational change, or allosteric transition, that alters a protein s activity or affinity for other ligands. [Pg.86]


See other pages where Allostery Inhibitors is mentioned: [Pg.797]    [Pg.475]    [Pg.126]    [Pg.1653]    [Pg.2338]    [Pg.475]    [Pg.608]    [Pg.115]    [Pg.154]    [Pg.139]    [Pg.29]    [Pg.244]    [Pg.232]    [Pg.313]    [Pg.45]    [Pg.26]   
See also in sourсe #XX -- [ Pg.93 ]




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