Conclusion:

In conclusion, the heat, altering pH, and adding a different solvent are agents which can cause protein
denaturation. Heat and various forms of solvents disrupt hydrogen bonds and hydrophobic non-polar
interactions can also be broken by heat. Acids, alkaloid reagents, etc. disrupt salt bridges. Evidence is
given to demonstrate the denaturation of heat. Proteins are the same a method as protein denaturation at
normal temperatures, dilute acids and alkalis and. Hydrolysis is the underlying reaction. The structure of
the protein can also be affected by heat. Applying heat to the protein molecule will interrupt the hydrogen
bonding and the non-polar hydrophobic interactions. The molecules are given additional energy such that
the weak ties that keep the protein together appear to unfold. Polar substances possibly react because the
hydrophobic region is in aqueous solutions exposed and unstable. We also conclude that the products of
denaturation of proteins by acids and by alkalis are different. The danger of using acids and alkalis and
prolonged dialysis in the preparation of proteins is emphasized. Denaturation is a process in which a
proteins lose the secondary structure, tertiary structure, and quaternary structure present in their native
state. It can be done by applying some external stress or compound such as concentrated inorganic salt,
strong acid, and an organic solvent, such as alcohol or chloroform, radiation, or heat. If a protein in a
living cell undergoes denaturation, this will disrupt cell activity and possibly cell death: Heat or radiation
supplies kinetic energy to the protein molecules, which will cause their atoms to vibrate more rapidly and
disrupt relatively weak hydrogen bonding and dispersion forces. Inorganic compounds can engage in
intermolecular hydrogen bonding with the protein molecule, which disrupts intramolecular hydrogen
bonding within the protein. Salts that form strong bonds with the carboxylate anions of the acidic amino
acids or SH groups of cysteine will disrupt the disulfide linkages and ionic bonds. Alkaloid reagents can
combine with positively charged amino groups in proteins to disrupt ionic bonds. Protein Denaturation
can also exhibit a wide range of characteristics, from conformational change to loss of solubility to
aggregation due to hydrophobic groups' exposure. When proteins are denatured and lose their 3D
structure, it cannot function properly.

Realization
One benefit of protein denaturation is that we can digest our food easily by cooking or adding heat to food
because the food's tertiary and secondary protein structure is already destroyed before we use it. Before
entering the body, a denatured protein has already been broken up and not broken by acids in the
stomach. It is also beneficial if you want to improve your protein levels. Denaturation leads to a loss of
protein activity during activity. Since native conformation is typically the most water-soluble structure, it
induces solubility changes and sometimes contributes to forming a solid solution. Reagents or conditions
that can cause denaturation are called denaturing agents; these include heat, pH changes, alcohol, and
heavy metal salts. Insofar, there is no problem encountered during this activity because all the details we
needed are included in the material given to us.
RESEARCH QUESTION
If your protein model (the model constructed in lecture) gets denatured by heat or agitation, what do you
think will happen to its solubility in water, viscosity and chemical reactivity? Explain your answers based
on relevant biochemical concepts and principles.

The protein still becomes insoluble, i.e., denatured, when a protein solution is heated and remains
insoluble even when the solution is cooled. When an egg-white protein is heated and an egg is boiled; it is
an example of inevitable denaturation. The denatured protein is similar to the original or native protein.
Chaperone proteins (or chaperonins) are helper proteins that provide favorable conditions for protein
folding to take place. The chaperonins clump around the forming protein and prevent other polypeptide
chains from aggregating. Once the target protein folds, the chaperonins disassociate. Although at high
temperatures, the weak forces between loaded groups and weaker forces of mutual attraction of non-polar
groups are disrupted; as a result, the protein's tertiary structure is lost. Proteins denature as the
temperature increases to the range that the DG curve for benzene reaches a peak. If the hydrophobic
residues behave like benzene they would like to stay buried and not flip out into water as the temperature
rises to the maximum in the DG curve. Hence this predicts that the protein should become more stable.  In
certain cases the original protein structure can be regenerated and the process is called renaturation. Some
of the biological processes, such as muscular contraction, which there is some reason to believe are
accompanied by denaturation are also accompanied by a gross increase in viscosity. It might be supposed
that the viscosity change are a result of denaturation. If, however, the viscosity change due to denaturation
is, in general, due to aggregation, then since aggregation is not peculiar to denatured proteins, an increase
in viscosity cannot by itself be taken as proof of denaturation. The proof that denaturation occurs
biologically must come from tests more specific for denaturation. The viscosity of a protein solution is
increased by the denaturation of the protein. This is true both when there is the formation of protein
aggregates which occlude water and when there is no aggregation. Under certain conditions, as a result of
the aggregation following denaturation, a solution containing only one per cent of protein may be
converted into a clear gel. The conditions for obtaining very viscous solutions containing little denatured
protein are always close to the conditions for actual precipitation and under these conditions the viscosity
is very sensitive to slight changes in the concentration of salts and hydrogen ions. Since denaturation
reactions are not strong enough to break the peptide bonds, the primary structure (sequence of amino
acids) remains the same after a denaturation process. Denaturation disrupts the normal alpha-helix and
beta sheets in a protein and uncoils it into a random shape. Virtually all studies of the protein-folding
reaction add either heat, acid, or a chemical denaturant to an aqueous protein solution in order to perturb
the protein structure. When chemical denaturants are used, very high concentrations are usually necessary
to observe any change in protein structure. In a solution with such high denaturant concentrations, both
the structure of the protein and the structure of the solvent around the protein can be altered.

Reference:

Libretexts. (2020, September 06). 7.7B: Denaturation and Protein Folding. Retrieved
Decemberv2, 2020, from
https://bio.libretexts.org/Bookshelves/Microbiology/Book:_Microbiology_(Boundless)/7:_
Microbial_Genetics/7.07:_Protein_Modification,_Folding,_Secretion,_and_Degradation/7.
7B:_Denaturation_and_Protein_Folding
Libretexts. (2020, September 01). F7. Hydrophobic Effect and Protein Denaturation. Retrieved
December 2, 2020, from
https://bio.libretexts.org/Bookshelves/Biochemistry/Book:_Biochemistry_Online_(Jakubo
wski)/02:_PROTEIN_STRUCTURE/2F:_Thermodynamics_and_IMF's_in_Protein_Stabili
ty/F07._Hydrophobic_Effect_and_Protein_Denaturation

Dunbar, J., Yennawar, H., Banerjee, S., Luo, J., & Farber, G. (1997, August). The effect of
denaturants on protein structure. Retrieved December 2, 2020, from
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143764/

Save Time and Improve your Marks with CiteThisForMe, The No. 1 Citation Tool. (n.d.).
Retrieved December 2, 2020, from https://www.citethisforme.com/topic-
ideas/chemistry/Biochemistry protein denaturation-44669161