EXPERIMENT 2B: PROTEIN DENATURATION
WHAT IS PROTEIN DENATURATION?
Protein denaturation is the partial or complete
disorganization of a protein’s characteristic three- EFFECT OF HEAT
dimensional shape.
Heat disrupts hydrogen bonds and non-polar
Result of disruption of its secondary, tertiary, and hydrophobic interactions.
quaternary structural interactions. Heat increases the kinetic energy and causes the
molecules to vibrate so rapidly and violently that the
Because the biochemical function of a protein depends on bonds are disrupted.
its three-dimensional shape, the result of denaturation is Proteins in eggs denature and coagulate during
loss of biochemical activity.
cooking, foods, are cooked to denature the proteins
Protein denaturation does not affect the primary structure of to make it easier for enzymes to digest them.
a protein.
Medical supplies and instruments are sterilized by
heating to denature proteins in bacteria and thus
destroy the bacteria.
High levels of thermal energy may disrupt the
hydrogen bonds that hold the protein together.
As these bonds are broken, the protein will begin to
unfold and lose its capacity to function as intended.
Temperatures at which proteins denature
Some proteins lose all of their three dimensional structural
may vary, but most human proteins function
characteristics upon denaturation, most proteins maintain
3D structure. optimally at body temperature.
Renaturation limited denaturation changes conditions can
be reversed, in which the protein is “refolded.”
EFFECT OF ALCOHOL
For extensive denaturation changes, the process is usually
irreversible. Hydrogen bonding occurs between amide groups in
Loss of water solubility is a frequent physical consequence the secondary protein structure.
of protein denaturation. Hydrogen bonding between “side chains” occurs in
Coagulation or precipitation out of biochemical solution of tertiary protein structure in a variety of amino acid
denatured protein. combinations.
Protein denaturation involves loss of the protein’s three- Alcohol denatures proteins by disrupting the side
dimensional structure. chain intramolecular hydrogen bonding.
Complete loss of such structure produces an “unstructured” protein
New hydrogen bonds are formed instead between
strand.
the new alcohol molecule and the protein side
chains.
70% alcohol solution is used as a
disinfectant on the skin.
70% of alcohol is able to penetrate the
bacterial cell wall and denature the
proteins and enzymes inside of the cell.
Angel Diang | BACHELOR OF NURSING
SAN PEDRO COLLEGE OF DAVAO
Page 7
95% alcohol solution merely coagulates the The negative charge of these anions counteracts the (+)
protein on the outside of the cell wall and charge of the amino group in proteins giving a precipitate.
prevents any alcohol from entering the cell.
EFFECT OF HEAVY METALS (CU, AG, BA)
Ions form strong bonds with the carboxylate
anions of the acidic amino acids or -SH groups
of cysteine, disrupting ionic and disulfide
linkages.
Heavy Metal Salts Disrupt Disulfide Bonds:
Heavy metals also disrupt disulfide
bonds because of their affinity and
attraction for sulfur and which lead to
the denaturation of proteins.
➢ Heavy metals can disrupt bonds in
the protein, causing it to lose its
structure.
Salts of heavy metals such as mercury and lead
may be used to denature … with protein’s
functional side chain groups to form complexes.
Heavy metals also oxidize the protein’s amino
acid side chains.
Heavy metals (e.g. Hg2+, Pb2+, Cu2+) are high
molecular weight cations.
(+) charge of cations counteracts the (-) charge
of the carboxylate group in proteins giving a
precipitate.
EFFECT OF STRONG ACIDS (H+)
Hydrogen bonding often involves these side chains.
Protonation of the amino acid residues changes whether or
not they participate in hydrogen bonding, so a change in the
pH can denature a protein.
All proteins have an optimal pH which is dependent
on the environment in which it functions.
Salt bridges result from the neutralization of an acid
and amine on side chains; interaction is ionic
between (+) amino group and (-) acid group.
EFFECT OF ALKALOIDAL REAGENTS
Alkaloidal reagents (e.g. tannate, picric & trichloroacetate)
are high molecular weight anions (-).
These reagents combine with (+) amino groups in proteins
to disrupt ionic bonds.
Angel Diang | BACHELOR OF NURSING
SAN PEDRO COLLEGE OF DAVAO
