Tag: proteins

Quizzes (22) Questions (29)

Questions Related to proteins

Multiple choice bio-chemistry proteins muscle tissue structure of protein muscle tissues

An example of structural protein is

  1. Myosin

  2. Collagen

  3. Keratin

  4. All of the above
Reveal answer Fill a bubble to check yourself
D Correct answer
Explanation

Structural proteins are fibrous proteins and form the largest class of proteins measured in terms of their total mass. Structural proteins include myosin, collagen, and keratin. 

Keratins form the protective covering like skin, hair, fur, wool, etc. in all land vertebrates. Equally widespread are the actin and myosin proteins of muscle tissue that play a major role in body movements. In addition, there are the collagens of tendons and hides, which form connective ligaments within the body.
Thus, the correct answer is option (D), 'All of the above'.

Multiple choice bio-chemistry proteins denaturation of protein proteins and amino acids proteins and enzymes

Primary structure of a protein is?

  1. sequence in which $\alpha-$ amino acids are linked to one another

  2. sequence in which amino acids of one polypeptide chain are joined to other chains

  3. the folding patterns of polypeptide chains

  4. the pattern in which the polypeptide chain are arranged
Reveal answer Fill a bubble to check yourself
A Correct answer
Explanation
The primary structure of a protein refers to the sequence of amino acids in the polypeptide chain. The primary structure is held together by peptide bonds that are made during the process of protein biosynthesis.
Multiple choice bio-chemistry proteins denaturation of protein proteins and amino acids proteins and enzymes

Most common types of secondary structures of proteins are?

  1. $\alpha-$ helix and $\beta-$ helix structures
  2. $\alpha-$ helix and $\beta-$ pleated structures

  3. right and left hand twisted structures

  4. globular and fibrous structures
Reveal answer Fill a bubble to check yourself
B Correct answer
Explanation
The most common types of secondary structures are the $\alpha$ helix and the $\beta$ pleated sheet. Both structures are held in shape by hydrogen bonds, which form between the carbonyl O of one amino acid and the amino H of another.
Multiple choice bio-chemistry proteins denaturation of protein proteins and amino acids proteins and enzymes

Proteins are found to have two different types of secondary structures vix. $\alpha-$ helix and $\beta-$ pleated sheet structure, $\alpha-$ helix structure of a protein is stabilised by:

  1. peptide bonds

  2. van der Waals forces

  3. hydrogen bonds

  4. dipole-dipole interactions
Reveal answer Fill a bubble to check yourself
C Correct answer
Explanation

Answer:- (C) hydrogen bonds

Two major factors stabilize the $\alpha$-helix structure are intrachain H-bonding and minimization of steric interference between side chains.

Multiple choice bio-chemistry proteins denaturation of protein proteins and amino acids proteins and enzymes

Cheese is a

  1. Glubular protein

  2. Conjugated protein

  3. Denatured protein

  4. Derived protein
Reveal answer Fill a bubble to check yourself
C Correct answer
Explanation

Cheese is a denatured protein. When producing (hard or semi-hard) cheese, the cheese yield can be increased by subjecting part of the cheese milk to a high temperature heat treatment. Thermal denaturation of whey proteins changes the protein structure so that part of the whey remains in the curd during the cheese-making process. 

Multiple choice bio-chemistry proteins denaturation of protein proteins and amino acids proteins and enzymes

Denaturation of proteins can be carried out by

  1. heat

  2. mineral acids

  3. bases

  4. all of the above
Reveal answer Fill a bubble to check yourself
D Correct answer
Explanation

Denaturation of proteins can be carried out by heat, mineral acids or bases. Denaturation is a process in which proteins lose their quaternary, tertiary and secondary structure which is present in their native state by application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent, radiation or heat. If proteins in a living cell are denatured, it results in disruption of cell activity and possibly cell death. Denatured proteins can exhibit a wide range of characteristics from loss of solubility to communal aggregation.

Multiple choice bio-chemistry proteins denaturation of protein proteins and amino acids proteins and enzymes

Enzymes are

  1. Carbohydrates

  2. Nucleic acids

  3. Globular proteins

  4. Fibrous proteins
Reveal answer Fill a bubble to check yourself
C Correct answer
Explanation

Option (C) is correct.
Enzymes are globular proteins, and catalyze metabolic reactions in living organisms.
They have a specific tertiary structure with an active site complementary to the substrate. They can speed up a reaction but do not get used up. Their activity can be affected by temperature and $pH$.

Multiple choice bio-chemistry proteins denaturation of protein proteins and amino acids proteins and enzymes

The type of bond that is most important in maintaining secondary structure of a protein is 

  1. disulphide bridges

  2. hydrogen bonding within the backbones
  3. hydrogen bonding between $R$ group

  4. salt bridges
Reveal answer Fill a bubble to check yourself
B Correct answer
Explanation
Secondary structure of a protein is generally maintained y hydrogen bonding between the $-NH$ group of one amide and the $C=O$ group of another amide
Multiple choice bio-chemistry proteins denaturation of protein proteins and amino acids proteins and enzymes

The sequence in which the $\alpha$-amino acids are linked to one another in a protein molecule is called its:

  1. primary structure

  2. secondary structure

  3. tertiary structure

  4. quaternary structure
Reveal answer Fill a bubble to check yourself
A Correct answer
Explanation

The primary structure of a protein is defined by the linear sequence of amino acids linked by peptide bonds. Secondary, tertiary, and quaternary structures refer to the folding and spatial arrangement of this chain.