Biology · Chemistry

Biomolecules and Enzymes

1,432 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. Biocatalysis

  2. Organocatalysis

  3. Heterogeneous catalysis

  4. Electrocatalysis

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

Biocatalysis is the use of natural catalysts, such as protein enzymes, to perform chemical transformations on organic compounds. Both enzymes that have been more or less isolated and enzymes still residing inside living cells are employed for this task.

Multiple choice
  1. Isoleucine

  2. Asparagine

  3. Leucine

  4. Lysine

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

Asparagine is one of the 20 most common natural amino acids on Earth. It has carboxamide as the side-chain's functional group. It is not an essential amino acid. Its codons are AAU and AAC.

Multiple choice
  1. fibronectin

  2. laminins

  3. osteonectin

  4. selectins

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

Osteonectin is a glycoprotein in the bone that binds sodium. It is secreted by osteoblasts during bone formation, initiating mineralization and promoting mineral crystal formation. Osteonectin also shows affinity for collagen in addition to bone mineral calcium.

Multiple choice
  1. creatine

  2. glycocyamine

  3. phosphocreatine

  4. creatinine

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

Glycocyamine is a metabolite of glycine in which the amino group has been converted into a guanidine. It is a direct precursor of creatine and is used as a supplement. However, the metabolism of creatine from glycocyamine in the liver causes a depletion of methyl groups.

Multiple choice
  1. Chemical specificity

  2. Communal aggregation

  3. Cooperative binding

  4. Pseudorotation

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

Cooperative binding is a special case of allostery. Cooperative binding requires that the macromolecule have more than one binding site, since cooperativity results from the interactions between binding sites.

Multiple choice
  1. Chymotrypsin

  2. Tyrosine

  3. Tryptophan

  4. Phenylalanine

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

Chymotrypsin is a digestive enzyme that can perform proteolysis. It is synthesized in the pancreas by protein biosynthesis as a precursor called chymotrypsinogen that is enzymatically inactive.