INI-CET EXAM -2026
Biochemistry & Nutrition
Medium

Assertion: The structural diversity of glycans exceeds that of proteins. Reason: Glycans are not assembled using a genetic template and can form branched chains with variable linkages.

Appeared in: INI-CET EXAM -2026

Explanation

  • The assertion is true: Glycans (carbohydrates) exhibit far greater structural complexity than proteins due to the combinatorial possibilities of their assembly.
  • The reason is also true: Unlike proteins, which are built from a genetic template into linear chains, glycans are synthesized enzymatically without a template.
  • This non-template synthesis allows for the formation of branched structures with various types of glycosidic bonds (e.g., α/β configurations, different carbon linkages like 1-4, 1-6).
  • Therefore, the reason correctly and directly explains the assertion. The lack of a template and the capacity for branching are the fundamental causes of the immense diversity of glycans.

Why Other Options Were Wrong

  • Option A: This option claims the Reason (R) is false. However, it is a fact that glycans are not assembled using a genetic template and can form branched chains.
  • Option B: This option claims the Assertion (A) is false. However, the structural potential of glycans is mathematically and biologically proven to be much larger than that of proteins.
  • Option D: This option correctly identifies that both statements are true but incorrectly claims that R is not the explanation for A. The ability to branch and use variable linkages (R) is the very definition of why glycan diversity (A) is so vast.

Related Visual

Visual explanation — Related Visual
Clinical Relevance
  • Nursing practice connection: This is primarily an exam-oriented knowledge point with limited direct bedside application, so retain Comparison of structural diversity between glycans and proteins as background academic context rather than a clinical decision trigger.
  • The ABO blood group system is a direct clinical application of glycan diversity. The A, B, and O antigens are specific carbohydrate structures on the surface of red blood cells.
  • Many viruses (like influenza) and bacteria use specific host cell surface glycans as receptors to initiate infection. The diversity of these glycans influences host susceptibility.
  • Changes in glycosylation patterns on cell surfaces are a hallmark of cancer. These altered glycans can be used as biomarkers for diagnosis and are targets for therapy.
How to Approach the Question
  • This is an Assertion-Reason question. Follow a systematic, three-step approach.
  • Step 1: Evaluate the Assertion (A). Read the statement 'The structural diversity of glycans exceeds that of proteins' and determine if it is true or false based on your knowledge of biochemistry.
  • Step 2: Evaluate the Reason (R). Read the statement 'Glycans are not assembled using a genetic template...' and determine if it is true or false.
  • Step 3: Evaluate the link. If both A and R are true, ask yourself: 'Does R correctly explain A?' In this case, ask 'Is the lack of a template and the ability to branch the reason why glycans are so diverse?'
  • Based on this analysis, select the option that matches your conclusions. If A and R are true and R explains A, the answer is C.
Concept Tested & Keywords
  • Concept Tested: Comparison of structural diversity between glycans and proteins
  • Stem keywords: glycans, proteins, structural diversity, genetic template, branched chains, variable linkages
  • Lead-in keywords: Assertion, Reason, correct explanation

Question ID

QSI3Dihkh7yuMn-vHb4nlK

Reference Book

E6 Harper's Illustrated Biochemistry2023 (pp 26-793 of 813) pp. 542-544, 138-140

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