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A protein becomes denatured when its normal shape ( Egg white) gets deformed because some of the
hydrogen bonds are broken. Weak hydrogen bonds break when too much heat is applied or when they
are exposed to an acid (like Rubbing Alcohol). As proteins deform or unravel parts of structure that
were hidden away get exposed and form bonds with other protein molecules, so they coagulate (stick
together) and become insoluble in water. I therefore conclude that When a protein is denatured, it
disrupts the hydrogen, ionic, and disulfide bridges within it, as well as affecting its temperature, pH
(hydrogen structure) and salinity.Some proteins can return to their original shape after denaturation,
while others cannot like from what happen to the rubbing alcohol and to the normal water and boiling
water whereas it state there changing structures.
After experiment. can dena protein occurs when the protein is subjected to intense conditions that
changes its secondary, tertiary, and quaternary structures like from what happen to the egg white,
however, the amino acid sequence or primary structure of the protein stays the same. The conditions to
denature a protein can be excessive heat, hugh low pH, to high an ionic strength, heavy metal ions,
organic solvents, or too vigorous stirring. The denatured protein may appear white for example, egg
white changes from clear to white when it pour to the rubbing alcohol. and in denatured. For the water
and boiling water we can determine that they are not denatured because no visible change occurred, in
all denatured test tubes precipitate was formed that was thick However, in these glass no significant
change occurred, and the color stayed the same therefore proving to us that they are not denatured.
With Glass for rubbing alcohol tubes states that the change was noticeable and that there was
precipitate being formed, allows us to understand that the proteins were denatured.