Yes.
Denaturation of a protein involves conformational changes. It involves the breaking of many of the weak linkages, or bonds such as hydrogen bonds, disulfide bonds, salt bridges etc. within a protein molecule. In an a -helix, the carbonyl of one amino acid is hydrogen bonded to the amino H (N-H) of an amino acid that is four down the chain and in a "\\beta" -pleated sheet, two or more segments of a polypeptide chain line up next to each other, forming a sheet like structure held together by hydrogen bonds. So when the structure of the fibrous protein is changed from "\\alpha" -helix to "\\beta" -pleated sheet structure, change in conformation, hydrogen bonding as well as in their secondary structure occurs, so the protein is said to be denatured.
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