Biology · Chemistry

Biomolecules and Enzymes

1,501 Questions

This topic focuses on biomolecules, specifically proteins, enzymes, and amino acids. It includes questions on enzyme structures, protein folding, and catalysis. These concepts are crucial for medical and biology competitive exams.

Enzyme catalysisProtein structuresAmino acid synthesisPolypeptide chainsBiomolecule properties

Biomolecules and Enzymes Questions

Multiple choice
  1. Proline

  2. Serine

  3. Glycine

  4. Histidine

Reveal answer Fill a bubble to check yourself
C Correct answer
Explanation

Glycine is the simplest amino acid because its side chain is just a single hydrogen atom, making it the only achiral amino acid.

Multiple choice
  1. Side chains

  2. Peptide bond

  3. Nitrogen atom

  4. Asymmetric carbon atom

Reveal answer Fill a bubble to check yourself
A Correct answer
Explanation

The polypeptide backbone consists of the repeating N-Calpha-C sequence. The side chains (R-groups) are attached to the alpha-carbon but are not considered part of the backbone itself.

Multiple choice
  1. L-stereo isomers

  2. D-stereo isomers

  3. No isomerism seen

  4. Enantiomers

Reveal answer Fill a bubble to check yourself
A Correct answer
Explanation

In biological systems, proteins are synthesized using only L-amino acids, which are the L-stereoisomers.

Multiple choice
  1. Metal (like Zn++ or Mg++) attached to the protein part of an enzyme

  2. Protein part of an enzyme

  3. Organic molecule attached to protein part of an enzyme

  4. Complete enzyme molecule

Reveal answer Fill a bubble to check yourself
C Correct answer
Explanation

A prosthetic group is a non-protein organic molecule or metal ion that is tightly or covalently bound to an enzyme and is essential for its catalytic activity.

Multiple choice
  1. Arginine

  2. Histidine

  3. Glutamic acid

  4. Glycine

Reveal answer Fill a bubble to check yourself
D Correct answer
Explanation

Glycine has a hydrogen atom as its side chain. Since it has two identical substituents (two hydrogens) on the alpha-carbon, it is achiral and not optically active.

Multiple choice
  1. they contain β strands only

  2. they contain α-helices interspersed with β-strands

  3. they are twisted in a left-handed helix instead of the usual right-handed one

  4. none of these

Reveal answer Fill a bubble to check yourself
B Correct answer
Explanation

Globular proteins often contain complex secondary structures, including both alpha-helices and beta-strands. Beta-conformation refers to the presence of beta-sheets or strands within the protein structure.

Multiple choice
  1. Folded polypeptide chain

  2. Unfolded polypeptide chain

  3. Polypeptide chain liked with disulphide bonds

  4. Polypeptide chain linked with weak covalent bonds

Reveal answer Fill a bubble to check yourself
B Correct answer
Explanation

Denaturation is the process where a protein loses its native three-dimensional folded structure. This results in an unfolded polypeptide chain, rendering the protein biologically inactive.

Multiple choice
  1. viral

  2. bacterial

  3. protozoan

  4. fungal

Reveal answer Fill a bubble to check yourself
A Correct answer
Explanation

Interferons are signaling proteins released by host cells in response to the presence of several viruses, acting as antiviral agents.