Enzyme/ja: Difference between revisions

Enzymes are not rigid, static structures; instead they have complex internal dynamic motions – that is, movements of parts of the enzyme's structure such as individual amino acid residues, groups of residues forming a [[turn (biochemistry)|protein loop]] or unit of [[protein secondary structure|secondary structure]], or even an entire [[protein domain]]. These motions give rise to a [[conformational ensemble]] of slightly different structures that interconvert with one another at [[thermodynamic equilibrium|equilibrium]]. Different states within this ensemble may be associated with different aspects of an enzyme's function. For example, different conformations of the enzyme [[dihydrofolate reductase]] are associated with the substrate binding, catalysis, cofactor release, and product release steps of the catalytic cycle, consistent with [[catalytic resonance theory]].