Castro, Clint Charles Q.

BS PSYCHOLOGY 2B

BIOCHEM LAB

1. Define denaturation

Denaturation, in biology, process modifying the molecular structure of a protein.

Denaturation involves the breaking of many of the weak linkages, or bonds (e.g.,
hydrogen bonds), within a protein molecule that are responsible for the highly ordered
structure of the protein in its natural (native) state. Denatured proteins have a looser,
more random structure; most are insoluble. Denaturation can be brought about in various
ways—e.g., by heating, by treatment with alkali, acid, urea, or detergents, and by
vigorous shaking.

2. What physical and chemical agents are capable of denaturing proteins? Give the type of
bonds or attractive forces disrupted by these agents.

1. Physical agents:
Heat, surface action, ul-traviolet light, ultrasound, high pressure etc.

2. Chemical agents:
Acids, alkalis, heavy metal salts, urea, ethanol, guanidine de-tergents etc. Urea and
guanidine probably interfere with the hydrogen bonds between peptide linkages. Acids
and alkalis probably attack directly the hy-drogen bonds in the secondary and tertiary
struc-ture of proteins.

REFERENCE:
https://www.britannica.com/science/denaturation
http://www.biologydiscussion.com/proteins/denaturation-of-proteins-with-denaturing-
agents/41902
Taopa, Adrian A.
BS PSYCHOLOGY 2B

BIOCHEM LAB

1. Define denaturation

Denaturation is a process in which proteins or nucleic acids lose the quaternary

structure, tertiary structure, and secondary structure which is present in their native state,
by application of some external stress or compound such as a strong acid or base, a
concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), radiation or
heat. If proteins in a living cell are denatured, this results in disruption of cell activity and
possibly cell death. Protein denaturation is also a consequence of cell death. Denatured
proteins can exhibit a wide range of characteristics, from conformational change and loss
of solubility to aggregation due to the exposure of hydrophobic groups. Denatured
proteins lose their 3D structure and therefore cannot function.

2. What physical and chemical agents are capable of denaturing proteins? Give the type of
bonds or attractive forces disrupted by these agents.

Physical agents:
• Heat
• Violent shaking
• X-rays
• Hydrostatic Pressure
• UV radiation

Chemical agents:
• Acids and alkalies
• Organic solvents
• Salts of heavy metals
• Chaotropic agents
• Detergents
• Altered pH

REFERENCE:
https://en.wikipedia.org/wiki/Denaturation_(biochemistry)
https://www.slideshare.net/spminal/denaturation-of-protein