Diosel Rezia M.

Praza
BSN-1B

REACTION PAPER
DENATURATION OF HUMAN HAIR

Although human hair has a complicated morphology as a -keratinous fiber, it can be

viewed in the perspective of thermal analysis as a nano-structured filament/matrix
composite. The performance of the -helical protein fraction during denaturation and the
results of reductive treatments were investigated using differential scanning calorimetry
(DSC) in water. The findings are interpreted in light of an earlier investigation into
oxidative therapies. According to an irreversible, one-step, first-order process, it was
discovered that the treatment had little to no effect on the course of denaturation.
Arrhenius activation energies and pre-exponential factors were calculated from the DSC
curves using the Friedman method. Comparing the activation energy values of oxidative
and reductive processes reveals the differences in the effects on the constituents of the
composite. However, although having different tendencies with cumulative treatments,
the values of the rate constant at the denaturation temperature are quite similar. This
underlines the idea that precise kinetic control over the denaturation of the -helical
segments is affected by the matrix's viscosity. When the matrix's viscosity is low enough
for denaturation to start, the process proceeds in a manner that is essentially unaffected
by temperature range and chemical prehistory.

Thermal equipment may be used during hair-straightening procedures, which has the
potential to harm the cuticle and cortex of the hair fibers. Heat specifically causes the
components of the hair cortex to degrade and the -keratin to become denatured.

In my perspective, a protein is said to be denatured when certain hydrogen bonds are

disrupted, causing the protein to lose some of its regular shape. When weak hydrogen
bonds are subjected to an acid or too much heat, they will break (like citric acid from
lemon juice). Numerous proteins, including egg white, are permanently denaturalized.
Loss of biological activity is a frequent side effect of denaturation.I discovered that while
a protein is denaturing, it starts to unfold and lose its three-dimensional form. This is
crucial because it gives digestive enzymes easier access to the protein links.
Denaturation is frequently reversible. Since proteins have an intact primary structure,
they can return to their native state by folding to the original conformation once the
denaturing impact has been eliminated. Renaturation is the name given to this
process.The hydrogen bonds that hold two strands of double-stranded DNA together
weaken and eventually break when a DNA solution is heated sufficiently. DNA can be
denatured using heat in a process that is very similar to melting. DNA denaturation is
the process of splitting double-stranded DNA into single strands. The DNA is heated
until it unwinds and divides into two single strands. The DNA will then be cooled back
down to a stable temperature once the strands have been separated.