<Li> In secondary structure denaturation, proteins lose all regular repeating patterns such as alpha - helices and beta - pleated sheets, and adopt a random coil configuration . </Li> <Li> Primary structure, such as the sequence of amino acids held together by covalent peptide bonds, is not disrupted by denaturation . </Li> <P> Most biological substrates lose their biological function when denatured . For example, enzymes lose their activity, because the substrates can no longer bind to the active site, and because amino acid residues involved in stabilizing substrates' transition states are no longer positioned to be able to do so . The denaturing process and the associated loss of activity can be measured using techniques such as dual polarization interferometry, CD, QCM - D and MP - SPR . </P> <P> In many cases, denaturation is reversible (the proteins can regain their native state when the denaturing influence is removed). This process can be called renaturation . This understanding has led to the notion that all the information needed for proteins to assume their native state was encoded in the primary structure of the protein, and hence in the DNA that codes for the protein, the so - called "Anfinsen's thermodynamic hypothesis". </P>

When was the enzyme most likely to be denatured
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