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the interactions between two proteins such as an antibody and an antigen or a hormone and its receptor are quite strong despite the fact that these interactions consist of relatively weak noncovalent bonds. how can this be?

Respuesta :

This observation is explained by the concept of molecular complementarity.

Concept of molecular complementarity.

Because there are so many noncovalent interactions happening when proteins, such as an antibody and an antigen, match up in a way that creates many noncovalent bonds, even weak noncovalent bindings can effectively produce strong interactions between two proteins.

When the structures of molecules or macromolecules fit together, physical, non-covalent interactions cause them to associate reversibly with one another. This is known as molecular complementarity.

Why is molecular complementarity significant in biomolecules?

Functions including information translation and storage, enzymatic operations, structural self-organization, and molecule defense against deteriorative processes all depend on molecular complementarity.

learn more about complementarity here

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