<Ul> <Li> In quaternary structure denaturation, protein sub-units are dissociated and / or the spatial arrangement of protein subunits is disrupted . </Li> <Li> Tertiary structure denaturation involves the disruption of: <Ul> <Li> Covalent interactions between amino acid side - chains (such as disulfide bridges between cysteine groups) </Li> <Li> Non-covalent dipole - dipole interactions between polar amino acid side - chains (and the surrounding solvent) </Li> <Li> Van der Waals (induced dipole) interactions between nonpolar amino acid side - chains . </Li> </Ul> </Li> <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> </Ul> <Li> In quaternary structure denaturation, protein sub-units are dissociated and / or the spatial arrangement of protein subunits is disrupted . </Li> <Li> Tertiary structure denaturation involves the disruption of: <Ul> <Li> Covalent interactions between amino acid side - chains (such as disulfide bridges between cysteine groups) </Li> <Li> Non-covalent dipole - dipole interactions between polar amino acid side - chains (and the surrounding solvent) </Li> <Li> Van der Waals (induced dipole) interactions between nonpolar amino acid side - chains . </Li> </Ul> </Li> <Ul> <Li> Covalent interactions between amino acid side - chains (such as disulfide bridges between cysteine groups) </Li> <Li> Non-covalent dipole - dipole interactions between polar amino acid side - chains (and the surrounding solvent) </Li> <Li> Van der Waals (induced dipole) interactions between nonpolar amino acid side - chains . </Li> </Ul>

Which of the following is an example of denaturation