Which of the following amino acids is classified as nonpolar and hydrophobic?
Q.82Easy
Collagen's characteristic triple helix structure is stabilized by which type of bonding?
Q.83Easy
Which cofactor is essential for the catalytic activity of lactate dehydrogenase (LDH)?
Q.84Easy
What is the primary function of chaperone proteins in the endoplasmic reticulum?
Q.85Easy
Which statement about peptide bonds is correct?
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Q.86Medium
In competitive enzyme inhibition, which Michaelis-Menten parameter is affected?
Q.87Medium
Which amino acid's deficiency in the diet can lead to kwashiorkor in children?
Q.88Medium
The Ramachandran plot is used to validate which aspects of protein structure?
Q.89Medium
Which enzyme belongs to the transferase class (EC 2)?
Q.90Medium
A patient has elevated serum creatine kinase (CK). Which tissue type is primarily affected?
Q.91Medium
Which prosthetic group is found in cytochrome c oxidase?
Q.92Medium
In a temperature vs. enzyme activity graph, why does enzyme activity decrease above the optimal temperature?
Q.93Medium
Which proteolytic enzyme is responsible for activating trypsinogen to trypsin in the small intestine?
Q.94Hard
A student observes that an enzyme shows sigmoidal kinetics instead of Michaelis-Menten kinetics. What does this indicate?
Q.95Hard
How does the proteasome recognize proteins marked for degradation in the ubiquitin-proteasome system?
Q.96Hard
A mutation changes a hydrophobic valine residue to a charged aspartate in the hydrophobic core of a globular protein. What is the most likely consequence?
Q.97Hard
A protein exhibits a β-sheet structure rich in proline residues. Why is this structurally problematic?
Q.98Hard
Which scenario best describes non-competitive enzyme inhibition kinetically?
Q.99Medium
A researcher studying protein folding observes that a newly synthesized polypeptide chain contains multiple disulfide bonds between cysteine residues. Which cellular compartment is most likely responsible for facilitating the formation of these disulfide bonds?
Q.100Medium
An enzyme exhibits a Km of 2 mM and Vmax of 100 μmol/min. When substrate concentration is 6 mM and an allosteric inhibitor is added, the Vmax decreases to 50 μmol/min while Km remains unchanged. What type of inhibition is occurring?
