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
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Glycine
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Tryptophan
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Leucine
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Methionine
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Cysteine
B
Correct answer
Explanation
It is required for the formation of nicotinamide.
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During synthesis of proteins
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During synthesis of disaccharides
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During synthesis of long chain fatty acids
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During synthesis of polynucleotides
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During synthesis of vitamins
A
Correct answer
Explanation
The bond formed between two amino acids is called peptide bond. A protein molecule is made of many amino acids linked together by peptide bond.
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LMP1
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NSP2
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HBx
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HBcAg
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HBsAg
A
Correct answer
Explanation
LMP1 is the best-documented oncoprotein of the Epstein–Barr virus (EBV), latent gene products.
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quaternary
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tertiary
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secondary
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primary
C
Correct answer
Explanation
The alpha-helix is a type of secondary protein structure. Secondary structure refers to local folding patterns stabilized by hydrogen bonds between the backbone amide and carbonyl groups. The alpha-helix and beta-sheet are the two main types of secondary structure. Primary structure is the amino acid sequence, tertiary is overall 3D folding, and quaternary involves multiple polypeptide chains.
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oxidation
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denaturation
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dehydration synthesis
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hydrolysis
C
Correct answer
Explanation
Dehydration synthesis (also called condensation) joins amino acids by removing a water molecule between them, forming peptide bonds that create polypeptide chains and enzymes. Oxidation involves electron loss, denaturation unfolds proteins, and hydrolysis breaks them down.
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Cyclooxygenase
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Bacteriorhodopsin
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Porins
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Maltoprotein
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None of these
A
Correct answer
Explanation
The target of aspirin action. Its hydrophobic helices do not span the whole membrane but interact strongly with the acyl groups on one side of the bilayer.
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1 only
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2 only
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3 only
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1 and 2
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2 and 3
A
Correct answer
Explanation
Fibrillin is a glycoprotein, which is essential for the formation of elastic fibers found in connective tissue.
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Actin
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Keratin
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Lignin
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Chitin
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Collagen
A
Correct answer
Explanation
Actin is a globular multi-functional protein that forms microfilaments.
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Leucine
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Proline
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Arginine
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Astacin
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None of these
A
Correct answer
Explanation
Leucine is the only dietary amino acid that has the capacity to stimulate muscle protein synthesis.
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Carbohydrates
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Fats
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Proteins
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Nucleic acids
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Inorganic compounds
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Enzyme + prosthetic group
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Enzymes having the same function, but a different molecular configuration are called holoenzymes
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Inactive form of enzymes
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The protein part of an enzyme
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Non-protein part of an enzyme
D
Correct answer
Explanation
The protein part of an enzyme is called apoenzyme, to which the coenzyme attaches to form an active enzyme.
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Concentration of substrate
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Affinity of an enzyme for its substrate
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Both (1) and (2)
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It is the t1/2 of the reaction.
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The rate at which ES complex dissociates to form the product.
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Inhibition of enzyme activity at an active site by an inhibitor which is structurally similar to a substrate
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Inhibition of first step of biosynthesis by the end-product of reaction
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Inhibition by a structurally different inhibitor at a place other than active site
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Denaturation of enzyme
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Mixed competitive and non-competitive inhibition
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Feedback inhibition
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Competitive inhibition
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Non-competitive inhibition
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Zymogen activation
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Denaturation
C
Correct answer
Explanation
Urease is highly sensitive to these metal ions and these ions non-competitively inhibit urease at some site other than the active site. Therefore, it is non-competitive inhibition.
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Apoenzyme
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Holoenzyme
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Pro-enzyme
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Isoenzyme
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Exoenzyme