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ICAR AICE-JRF/SRF General Biochemistry & Metabolism: practice questions

ICAR AICE-JRF/SRF (PhD) — Food Processing Technology, Food Safety & Quality, Processing and Food Engineering · India · ICAR through the National Testing Agency

Original practice questions written to the published syllabus · not past papers
7worked here, free
16written to this exam in this subject
10syllabus units

What this subject covers

The structure of biomolecules and the metabolic pathways that turn food into energy and body tissue. Food chemistry (phase 2) describes how these molecules behave in a food; this subject explains how they behave in the body and in living raw materials such as respiring fruit and post-mortem muscle.

In the exams: ICAR AIEEA-PG Code 18 Unit I (metabolism of carbohydrates, lipids and protein; BV and PER)

Where the 16 questions fall

How our questions for ICAR AICE-JRF/SRF spread across the units of General Biochemistry & Metabolism. Difficulty: 0 easy, 5 medium, 11 hard.

Biochemistry of post-harvest respiration and post-mortem muscle3
Enzymes: classification, mechanism, Michaelis-Menten kinetics and inhibition2
Bioenergetics, ATP and the electron transport chain2
Nucleic acids, replication, transcription and translation2
Biochemical laboratory techniques: centrifugation, electrophoresis and spectrophotometry2
Coenzymes and vitamins as cofactors1
Carbohydrate metabolism: glycolysis, TCA cycle, gluconeogenesis and glycogen1
Lipid metabolism: beta-oxidation and fatty-acid synthesis1
Protein and amino-acid metabolism and the urea cycle1
Hormonal regulation of metabolism1

7 practice questions, worked

Choose an answer, then open the working. Each explanation says why the right answer is right and why the others are not.

1 · Enzymes: classification, mechanism, Michaelis-Menten kinetics and inhibition · hard

An allosteric enzyme gives a sigmoidal plot of rate against substrate concentration. What does this shape indicate?

  1. Cooperative binding between subunits
  2. That the enzyme follows Michaelis-Menten kinetics with a very low Km
  3. That substrate concentration was measured on a logarithmic scale
  4. That the enzyme has been irreversibly inhibited by the substrate
Answer and working

A. Cooperative binding between subunits

Sigmoidal kinetics arise when binding at one site changes the affinity of others, as in multi-subunit regulatory enzymes; the Michaelis-Menten equation, which gives a hyperbola, does not apply. Irreversible inhibition lowers activity overall; a log scale makes even a hyperbola look sigmoidal, but the question concerns a plot against concentration.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

2 · Enzymes: classification, mechanism, Michaelis-Menten kinetics and inhibition · hard

An assay containing 1.0 µM enzyme reaches Vmax = 600 µM of product per minute. What is kcat?

  1. 10 s⁻¹
  2. 36000 s⁻¹
  3. 0.1 s⁻¹
  4. 600 s⁻¹
Answer and working

A. 10 s⁻¹

kcat = Vmax/[E]total = 600 µM min⁻¹/1.0 µM = 600 min⁻¹ = 10 s⁻¹. 600 s⁻¹ forgets to convert minutes to seconds; 36 000 s⁻¹ multiplies by 60 instead of dividing; 0.1 s⁻¹ inverts the ratio.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

3 · Bioenergetics, ATP and the electron transport chain · medium

2,4-Dinitrophenol increases oxygen consumption by mitochondria while ATP synthesis falls. Why?

  1. It reduces oxygen to water without any electron carriers
  2. It blocks complex I, forcing electrons to bypass to complex III
  3. It carries protons across the membrane, collapsing the gradient
  4. It inhibits ATP synthase directly, so ADP accumulates
Answer and working

C. It carries protons across the membrane, collapsing the gradient

As an uncoupler, dinitrophenol shuttles protons back into the matrix, so electron transport runs fast with nothing to slow it, but no gradient remains to drive ATP synthase; the energy becomes heat. Blocking complex I would reduce oxygen uptake; oligomycin, not dinitrophenol, inhibits ATP synthase.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

4 · Protein and amino-acid metabolism and the urea cycle · hard

What is the main methodological advance of DIAAS over PDCAAS in protein-quality scoring?

  1. It uses faecal nitrogen digestibility of the whole protein, capped at 1.0
  2. It uses rat weight gain instead of human amino-acid requirements
  3. It ignores digestibility and scores only the amino-acid pattern
  4. It uses ileal digestibility of each amino acid, without truncation
Answer and working

D. It uses ileal digestibility of each amino acid, without truncation

The digestible indispensable amino acid score, recommended by FAO in 2013, corrects each indispensable amino acid for its own ileal digestibility, avoiding the overestimation that faecal digestibility gives, and reports values above 100% without truncation. PDCAAS uses faecal protein digestibility and is capped at 1.0; rat growth is the basis of PER.

Further reading: Lehninger Principles of Biochemistry; FAO Food and Nutrition Paper 92 (2013)

5 · Nucleic acids, replication, transcription and translation · medium

In PCR, what happens during the annealing step?

  1. The polymerase extends primers to copy the target sequence
  2. Primers bind to complementary sequences on single-stranded templates
  3. The product is visualised on a gel under ultraviolet light
  4. The double-stranded DNA is separated by heating to about 95 °C
Answer and working

B. Primers bind to complementary sequences on single-stranded templates

Annealing, at a temperature set by the primers, lets them hybridise to the template. Separation is denaturation; extension is the polymerase step; gel visualisation is after PCR.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

6 · Nucleic acids, replication, transcription and translation · medium

In the lac operon of Escherichia coli, what happens when lactose is present and glucose is absent?

  1. The repressor binds the operator and transcription stops
  2. Transcription is low, because catabolite repression is active
  3. The lac genes are spliced out of the messenger RNA
  4. The repressor is released and transcription of the lac genes is high
Answer and working

D. The repressor is released and transcription of the lac genes is high

Allolactose binds the repressor and removes it from the operator; with glucose absent, cAMP-CRP activates the promoter, so expression is high. Catabolite repression operates when glucose is present; bacterial genes are not spliced.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

7 · Biochemical laboratory techniques: centrifugation, electrophoresis and spectrophotometry · medium

Which technique combines separation by isoelectric point with separation by molecular mass?

  1. Western blotting alone
  2. Native agarose gel electrophoresis
  3. Gel filtration chromatography
  4. Two-dimensional gel electrophoresis
Answer and working

D. Two-dimensional gel electrophoresis

2D electrophoresis runs isoelectric focusing in the first dimension and SDS-PAGE in the second, resolving hundreds of proteins. Native agarose separates by size and charge of DNA or proteins; gel filtration by size; a Western blot detects specific proteins with antibodies after electrophoresis.

Further reading: Wilson and Walker, Principles and Techniques of Biochemistry and Molecular Biology

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General Biochemistry & MetabolismThe full study manual, free ICAR AICE-JRF/SRFFormat, sections and how it has changed

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