PROTEINS

SELF-LEARNING QUESTIONS:
1. What are the many functions of Proteins?
Ans: The body requires protein. It contributes to tissue repair, metabolic responses, and body
function coordination. Proteins not only sustain the structure but also help maintain the pH
and fluid balance.Finally, they aid in the immune system's function, transport and store
nutrients, and serve as a source of energy. Protein has a variety of tasks that contribute to its
importance as food for your health. Proteins are necessary for the growth and repair of
tissues. However, proteins undergo modification. When the body requires more protein than
it can create, such as during illness, pregnancy, or breastfeeding, the body breaks it down.
Enzymes are proteins that catalyze critical chemical reactions within the body. Proteins and
peptides are composed of amino acid chains that serve as a means of communication between
cells, tissues, and organs. Fibrous proteins provide structure, strength, and elasticity to your
body. Proteins operate as a buffer, allowing your body to maintain a proper pH level in your
blood and other bodily fluids. Blood proteins carry the fluid equilibrium between the blood
and the tissues. Antibodies are proteins that aid your body in defending itself against invaders
such as bacteria and viruses. Specific proteins are involved in transferring nutrients, whereas
others are involved in their storage for an energy source.

2. What are Amino acids?

Ans: Amino acids are a family of chemicals that are involved in a wide variety of bodily
processes. They are necessary for protein synthesis, hormone synthesis, and neurotransmitter
synthesis. The human body cannot produce critical amino acids because it lacks the metabolic
pathways required. Thus, essential amino acids (histidine, isoleucine, leucine, lysine,
methionine, phenylalanine, threonine, tryptophan, and valine) must be obtained through
dietary sources. On the other hand, non-essential amino acids including alanine, arginine,
asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine, and
tyrosine can be obtained by food.

3. What are Zwitterions?

Ans: The term 'Zwitterion' is derived from the German word 'zwitter,' which translates as
'hybrid' or 'hermaphrodite. A zwitterion is an ion having two functional groups. It is a double-
charged ion. As a result, zwitterions are predominantly electroneutral (the net formal charge
is usually zero). Zwitterions are frequently referred to as "inner salts." Rarely are dipolar
compounds zwitterions. On the amine oxide, the plus and minus symbols represent formal
charges. Zwitterions may be worth considering when working with acid, basic, or neutral
leads.

4. What determines the characteristics of Amino Acids?

Ans: The chemistry of the side chain dictates the characteristics of the amino acid. Valine,
methionine, and alanine are nonpolar amino acids, whereas serine, threonine, and cysteine are
polar amino acids (hydrophilic). Due to lysine and arginine's positively charged side chains,
they are called essential (high pH) amino acids. The R group of proline is linked to the amino
group, resulting in a ring-like shape. Amino acids are denoted by a single capital letter or
three capital letters. For instance, valine is indicated by the letters V or "val."

5. What are uncommon Amino Acids?

Ans: The carboxyl and amino groups are linked to the same carbon atom (the carbon). They
differ in their R group or side-chain group. The R-group determines the acid/basic nature,
solubility, stability, and ultimately the proteins. Organisms' proteins may contain changed
amino acid residues. Examples of 4-hydroxyproline are 5-hydroxylysine from lysine and -
carboxyglutamate from glutamic acid. Selenocysteine has selenium instead of cysteine's
sulfur. These amino acids are referred to as “uncommon.”

6. How do Amino Acids combine to form proteins?

Ans: Amino acids are the building blocks of proteins. All amino acids have a carboxyl (acid)
or COOH group. Proteins are composed of twenty amino acids, with each molecule
containing 300 or more amino acids. Each amino acid has a unique "R" group. The "R" group
in an amino acid refers to the molecule's components other than the amino acid and central
carbon. Each amino acid has its unique "R" group, which dictates its chemical properties.
Polypeptides and proteins are formed via peptide bonds between the amino or NH2 group of
one amino acid and the carboxyl (acid) or COOH group of another amino acid. A peptide is
an amino acid chain that has two or more peptide bonds. Proteins are constructed from
lengthy chains of amino acids that are connected by peptides.

7. What are the properties of proteins?

Ans: Proteins have no flavour. However, protein hydrolysates have a bitter taste. Proteins
have no smell. Proteins have several colloidal features due to their substantial molecular size
and are usually virtually neutral substances, neither acidic nor basic. The number of acidic
carboxyl (COO) groups in aspartic and glutamic acid is roughly equivalent to that of primary
carboxyl groups.

8. What is the primary structure of proteins?

Ans: The main structure of a protein is its amino acid sequence. Proteins are made up of only
twenty amino acids, each with its side chain. Amino acid side chains have various
chemistries. Most amino acids contain nonpolar side chains.

9. What is the tertiary structure of proteins?

Ans: A protein's tertiary structure is the overall three-dimensional organization of its
polypeptide chain. Hydrophobic interactions between nonpolar amino acid side chains
stabilize it.

10. What is the quartenary structure of a protein?

Ans: A protein's quaternary structure is formed by multiple protein chains or subunits tightly
packed together. They have distinct primary, secondary, and tertiary structures. Hydrogen
bonds and van der Waals forces hold the subunits together.
11. How are proteins denatured?
Ans: A protein is denatured when part of its hydrogen bonds break, causing it to lose its
natural structure. Proteins coagulate (stick together) and become insoluble in water as they
distort or unravel.