Denaturation of proteins involves the disruption of secondary, tertiary, and quaternary structures due to the breaking of non-covalent interactions (like hydrogen bonds, hydrophobic interactions, and ionic bonds). However, the primary structure — the linear sequence of amino acids held together by peptide bonds — remains unaffected. These covalent bonds are much stronger and are not broken during simple denaturation processes.
Hence, only the primary structure (1°) remains intact.