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===Conformational selection hypothesis===
This model suggests that enzymes exist in a variety of conformations, only some of which are capable of binding to a substrate. When a substrate is bound to the protein, the equilibrium in the conformational ensemble shifts towards those able to bind
==Types of non-covalent interactions==
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In the second stage, the R'NH group is protonated by His-57 to form [[Amine|R'NH<sub>2</sub>]] and leaves the intermediate, leaving behind the [[acyl group|acylated]] Ser-195. His-57 then acts as a base again to abstract one proton from a water molecule. The resulting [[hydroxide]] anion nucleophilically attacks the acyl-enzyme complex to form a second tetrahedral oxyanion intermediate, which is once again stabilised by H bonds. In the end, Ser-195 leaves the tetrahedral intermediate, breaking the CO bond that connected the enzyme to the peptide substrate. A proton is transferred to Ser-195 through His-57, so that all three amino acid return to their initial state.
==Cofactors==
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