Six Examples of Denaturing Proteins

Denaturation

refers to the physical changes that take place in protein exposed to abnormal conditions in the environment.

Organic Compounds

Acts as a disinfectants by exchanging the bacterial proteins hydrogen bonds to water with their own. Example: rubbing alcohol Used as a disinfectant b/c of its ability to coagulate the protein present in bacteria.

Acid/Bases

Changes pH proteins can be denatured by changing the pH. Example: Tannic acid *Changes in H+ causes a disruptions in H-bonds and salt bridges. Tannic acid is used in burn ointments and applied to the site of the burn to coagulate proteins that works as a protective cover and prevents future loss of fluid from the burn.

Heavy Metal Ions

Denature proteins by forming bonds with ionic residues of reacting with disulfide. Example: AgNO3 are placed in the eyes of newborns. Used to prevent eye infections such as gonorrhea in newborns and disrupts the salt bridges and the disulfide bonds.

Heat/Temperature

Disrupts H-bonds and hydrophobic interactions between non-polar reactions. Example: boiling The denatured proteins of eggs will lose enzyme biological action function, but nutritional balance value remains the same.

Agitation

Whipping with beaters--think of cream and egg whites. Example: Whisking egg whites to make angel food cake. The bubbly foam is what gives the angel food cake it's structure and denatures the protein.