The function of a protein is dependent upon the shape into which the chain of amino acids folds. many noncovalent interactions are responsible for maintaining the protein's shape. assume you have isolated a protein from an organism in its proper shape, and you have treated it with an enzyme that selectively targets and breaks only the peptide bonds in the proteins. would the protein retain its shape under these conditions? a. no; whereas the noncovalent bonds determine the shape of a protein, the peptide bonds are required to hold the amino acids together.
b. yes; the noncovalent interactions are stronger than the peptide bonds.
c. yes; once the shape of a protein is formed, the peptide bonds are unnecessary.
d. yes; but the shape would be affected to a greater extent by changes in temperature.

a. No; whereas the noncovalent bonds determine the shape of a protein, the peptide bonds are required to hold the amino acids together.

Explanation:

Proteins are the polymers of amino acids. Amino acids are joined together by peptide bonds to make long chains of polypeptides. Therefore, the peptide bonds maintain the primary structure of a protein. Once several amino acids are held together by peptide bonds, the polypeptide chains are folded into secondary, tertiary and quaternary structures.

Breaking the peptide bonds would digest the protein and release the amino acids from the polypeptide chain. Therefore, digestion of peptide bonds would break down the protein which in turn would not be able to maintain its shape in the absence of a polypeptide chain.

i think that is new experiments yield untrustworthy data and should be carefully considered, because you don't know what will happen with the experiments.