Home Subjects Biochemistry Proteins & Enzymes

Biochemistry
Proteins & Enzymes

Metabolic pathways, enzymes, proteins

27 Q 3 Topics Take Mock Test
Advertisement
Difficulty: All Easy Medium Hard 21–27 of 27
Topics in Biochemistry
All Proteins & Enzymes 100 Carbohydrates 100 Lipids 78
In non-competitive inhibition, what is the graphical representation on a Lineweaver-Burk plot?
A Lines intersect on the y-axis
B Lines intersect on the x-axis
C Lines intersect to the left of the y-axis
D Parallel lines
Correct Answer:  A. Lines intersect on the y-axis
EXPLANATION

In non-competitive inhibition, both Km and Vmax are affected proportionally. On a Lineweaver-Burk plot (1/v vs 1/[S]), this results in lines with different slopes that intersect on the y-axis.

Test
A protease enzyme shows reduced activity when Ca²⁺ is removed from the reaction mixture. This indicates that Ca²⁺ acts as a:
A Substrate
B Allosteric regulator
C Cofactor
D Competitive inhibitor
Correct Answer:  C. Cofactor
EXPLANATION

Ca²⁺ is required for enzymatic activity and is not consumed in the reaction, making it a cofactor. Many proteases require metal ions as structural or catalytic cofactors.

Test
Which statement about the relationship between protein structure and function is INCORRECT?
A Primary structure determines all higher-order structures
B Tertiary structure can exist without secondary structure
C Quaternary structure requires multiple polypeptide chains
D Disulfide bonds stabilize tertiary structure in extracellular proteins
Correct Answer:  B. Tertiary structure can exist without secondary structure
EXPLANATION

Tertiary structure requires secondary structure elements. Secondary structures (α-helix, β-sheet) fold into tertiary structure; one cannot exist without the other.

Test
A competitive inhibitor with Ki = 0.5 mM and Km = 2 mM is added to an enzyme reaction. What is the apparent Km in presence of this inhibitor at [I] = 1 mM?
A 2 mM
B 4 mM
C 6 mM
D 8 mM
Correct Answer:  C. 6 mM
EXPLANATION

Apparent Km = Km(1 + [I]/Ki) = 2(1 + 1/0.5) = 2(1 + 2) = 6 mM. Competitive inhibition increases apparent Km without changing Vmax.

Test
In a double displacement enzyme reaction mechanism, the enzyme forms a covalent intermediate. Which protease follows this mechanism?
A Pepsin
B Serine proteases
C Metalloproteases
D Cysteine proteases
Correct Answer:  B. Serine proteases
EXPLANATION

Serine proteases (like trypsin, chymotrypsin) form an acyl-enzyme intermediate through a nucleophilic attack by the active site serine residue.

Test
During protein synthesis, a missense mutation changes codon GAA to GUA. Which amino acid substitution occurs?
A Glutamic acid to Valine
B Aspartate to Leucine
C Glutamine to Isoleucine
D Glutamic acid to Alanine
Correct Answer:  A. Glutamic acid to Valine
EXPLANATION

GAA codes for Glutamic acid (Glu), GUA codes for Valine (Val). This is a non-conservative substitution of a charged to hydrophobic residue.

Test
A protein with multiple subunits shows cooperative binding of substrate. This phenomenon is best explained by:
A Competitive inhibition
B Allosteric regulation
C Non-competitive inhibition
D Covalent modification
Correct Answer:  B. Allosteric regulation
EXPLANATION

Cooperative binding (positive cooperativity) occurs when binding of one substrate molecule increases affinity for subsequent molecules, a classic example of allosteric regulation as seen in hemoglobin.

Test
IGET
IGET AI
Online · Exam prep assistant
Hi! 👋 I'm your iget AI assistant.

Ask me anything about exam prep, MCQ solutions, study tips, or strategies! 🎯
UPSC strategy SSC CGL syllabus Improve aptitude NEET Biology tips