The interactions of proteins that help determine the structure of a protein are affected by denaturation, except the covalent amide bonds of the primary structure.
By applying some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (such as alcohol or chloroform), agitation, radiation, or heat, proteins or nucleic acids lose the quaternary structure, tertiary structure, and secondary structure that are present in their native state.
Denatured proteins affect cellular function and may even cause cell death in living cells. Cell death also leads to protein denaturation. Denatured proteins can display a wide range of traits, including structural change, loss of solubility, and aggregation because hydrophobic groups are exposed. Coagulation describes the decrease of solubility brought on by denaturation.
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