MODULE 7 Amino

acids andProteins
Name: DANIELLA DE VERA
Course, Year and Section: BSMT-2 Date: NOVEMBER 18, 2022

Try answering this question before we proceed to our discussion. Which do you think came
first, the chicken or the egg? Why?
Based on what we know about proteins, I believe that eggs predate chickens. For instance, if
a form of life was evolving at the time the egg started to form, we can infer that there is a chance
that an egg could still be produced by a variety of processes that a particular DNA goes through,
such as transcription, where a gene's DNA is replicated into RNA, followed by translation, where
the RNA molecule acts as the code for the creation of a protein. Since no chicken lays eggs, we
can assert that having an egg is still conceivable thanks to the process of protein synthesis.

Now that we have read what protein and its structures are, let us now test our knowledge and
try to answer the following questions.

1. Why is it necessary to have proteins in our diet?

ANSWER:
Every cell in the human body contains protein. The basic structure of protein is a chain of
amino acids. You need protein in your diet to help your body repair cells and make new
ones. Protein is also important for growth and development in children, teens, and pregnant
women
2. Why are all amino acids solids at room temperature?
ANSWER:
they are internal salts, amino acids are all solids at room temperature, and most of
them are soluble in water. Not all amino acids are completely stable in powder form at
room temperature (e.g. The L-Lysine I have in the lab needs to be stored under 0
degrees: very hygroscopic). But you are right--most of them are.

ELABORATE
 Boiling a protein solution destroys the -helical and β-pleated sheet structure. In collagen,
the triple helixes disappear upon boiling, and the molecules have a largely random-coil
conformation in the denatured state, which is gelatin. In globular proteins, heat causes the
unfolding of the polypeptide chains; because of subsequent intermolecular protein-protein
interactions, precipitation or coagulation then takes place. An example of this is when we boil
eggs.

What changes in the physical state of the egg happens after boiling it?
ANSWER:
These proteins are folded and curled to form a tight ball in a raw egg. These proteins uncurl
and create new links with one another when you boil an egg. The proteins will connect to each
other more tightly when they are heated for a longer period of time and at a greater temperature,
which will cause the liquid state of the egg white and yolk to solidify and harden.
Is it reversible or irreversible denaturation? Why?
ANSWER:
The protein structure is uncurled and forms new bonds with one another, and because of the
intermolecular protein-protein interactions that cause the protein to coagulate inside the egg, the
protein cannot return to its native state by folding back to its original conformation. This is an
irreversible denaturation.

EVALUATE

GENERAL INSTRUCTIONS:
Browse the entire questionnaire before answering.
Choose and think of the best answer ALWAYS.
You are allowed to browse the web or scan your noted but NO copying or sharing
of answers with your classmates.
Write your final answer in your answer sheet when you are ready and sure.

I. Multiple Choice (2 pts each). Write the answer on the space provided.

A_____ 1. The three-dimensional spatial configuration of a single polypeptide chain

as determined by disulfide linkages, hydrogen bonds, electrostatic attractions, and van
der Waals forces is referred to as the
a. Tertiary structure c. Secondary structure
b. Primary structure d. Quaternary structure

A_____ 2. A peptide bond is

a. Amino group and carboxyl group bonded to the alpha-carbon
 b. A double carbon bond
c. A tertiary ring of amino group and carboxyl group bonded to the alpha-carbon
d. Two amino groups bonded to the alpha-carbon

D_____ 3. Which of the following is an example of tertiary structure in a protein?

a. polyalanine c. a -pleated sheet
b. an -helix d. a globular domain

A_____ 4. Disulfide bonds most often stabilize the native structure of:
a. extracellular proteins c. hydrophobic proteins
b. dimeric proteins d. intracellular proteins

C_____ 5. The fact that the core of most globular proteins is composed of non-polar
residues is because of
a. van der Waals interactions c. the hydrophobic effect
b. hydrogen bonds d. favorable electrostatic interactions

II. Essay (10 pts).

Denaturation is usually associated with transitions from helical structures to
random coils. If an imaginary process were to transform the keratin in your hair
from an -helix to a -pleated sheet structure, would you call the process
denaturation? Explain.

Yes. Protein denaturation involves conformational changes. It entails the dissolution of

numerous weak connections, or bonds, within a protein molecule, including hydrogen bonds,
disulfide bonds, salt bridges, etc. In an a-helix, an amino acid's carbonyl forms a hydrogen
bond with an amino acid four amino acids down the chain, called the amino H (N-H), and in a
"beta-pleated sheet," two or more polypeptide chain segments line up next to one another and
form a sheet-like structure that is held together by hydrogen bonds. The protein changes in
conformation, hydrogen bonding, and secondary structure when the structure of the fibrous
protein changes from an alpha-helix to a beta-pleated sheet structure.