1. 19.6 Protein Hydrolysis and Denaturation
Denaturation of a protein occurs when the interactions of residues that stabilize tertiary or quaternary structures are disrupted, which destroys the shape and renders the protein biologically inactive.
Learning Goal Describe the hydrolysis and denaturation
of proteins.

2. Protein Hydrolysis
Peptide bonds are broken through hydrolysis reactions. Hydrolysis
occurs in the stomach when enzymes catalyze the hydrolysis of proteins to give amino acids.
breaks up the primary structure by breaking the covalent peptide bonds that link the amino acids.

3. Protein Hydrolysis

4. Denaturation of Proteins
Denaturation of a protein
occurs when a change disrupts the interactions between residues that stabilize the secondary, tertiary, or quaternary structure.
does not affect the amide bonds between amino acids.

5. Denaturation of Proteins
The loss of secondary and tertiary structures in a protein occurs when conditions change, such as
increasing the temperature.
making the pH very acidic or basic.
adding certain organic compounds or heavy metal ions.
adding mechanical agitation.
When the interactions between the residues are disrupted,
a globular protein unfolds.
the tertiary structure is disrupted and the protein is no longer biologically active.

6. Denaturation of Proteins, Heat
Proteins are denatured when heated above 50 °C. The heat
disrupts the hydrogen bonds and hydrophobic interactions between nonpolar residues.
does not change the nutritional value of proteins but makes them more digestible.
High temperatures are also used to disinfect surgical instruments and gowns by denaturing the proteins of any bacteria present.

7. Denaturation of Proteins, Acids and Bases
Proteins can be denatured by changing the pH, which
breaks hydrogen bonds.
disrupts ionic bonds and salt bridges.
Tannic acid, a weak acid used in burn ointments, is applied to the site of the burn to coagulate proteins. It forms a protective cover and prevents further loss of fluid from the burn.

8. Denaturation of Proteins, Organic Compounds
Organic compounds such as ethanol and isopropyl alcohol act as disinfectants by
exchanging the bacterial protein’s hydrogen bonds to water with their own.
disrupting the side chain intramolecular hydrogen bonding.
An alcohol swab is used to clean wounds or to prepare the skin for an injection because the alcohol passes through the cell walls and coagulates the proteins inside the bacteria.

9. Denaturation of Proteins, Heavy Metal Ions
Heavy metal ions such as Ag+, Pb2+, and Hg2+ denature proteins by forming bonds with ionic residues or reacting with disulfide — S — S — bonds. Dilute (1%) solutions of AgNO3 are placed in the eyes of newborn babies to destroy the bacteria that cause gonorrhea.

10. Denaturation of Proteins, Agitation
The whipping of cream and the beating of egg whites are examples of using mechanical agitation to denature proteins. The whipping action stretches the polypeptide chains until the stabilizing interactions are disrupted.

11. Denaturation of Proteins, Summary

12. Concept Map