Practice Questions

60. The chemical nature of the linkage connecting the lipid anchor to the carbohydrate core in a glycosylphosphatidylinositol (GPI)-anchored protein is a

A. Phosphodiester and covalent bond framework
B. Reversible non-covalent hydrogen bond attraction
C. Purely ionic interaction between magnesium ions
D. Direct peptide linkage between fatty acids and sugars

GPI anchors use a complex bridge made of a phospholipid linked via a phosphodiester bond to an oligosaccharide, which then binds the protein.

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59. The structure of a nucleosome core particle involves a loop of double-stranded DNA wrapped around an octamer of histones, which represents a highly organized

A. Glycolipid sheet
B. Nucleoprotein complex
C. Lipoprotein vesicle
D. Chromoprotein filament

This structural packaging arranges DNA strands systematically inside the eukaryotic nucleus, compacting the genetic material.

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Ovalbumin is a storage glycoprotein that makes up the bulk of egg white, providing essential amino acids and attached carbohydrates.

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57. The introduction of an enzyme that selectively destroys the carbohydrate component of follicular stimulating hormone (FSH) will

A. Leave its receptor-binding affinity unchanged
B. Alter its tertiary shape and completely abolish its biological response
C. Convert it into a functional membrane glycolipid
D. Trigger immediate replication of the target cell genome

The carbohydrate arrays on glycoprotein hormones are essential for maintaining proper folding, structural stability, and receptor activation.

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56. The structural component that distinguishes a lipopolysaccharide from a standard glycolipid is that the lipopolysaccharide contains

A. No lipid components at all
B. A highly extended, complex core polysaccharide and O-antigen chain
C. A single simple monosaccharide unit attached to glycerol
D. A sequence of basic histone protein subunits

Standard glycolipids feature small oligosaccharide chains, whereas bacterial LPS molecules possess highly complex, extended carbohydrate structures.

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55. The presence of small nuclear ribonucleoproteins (snRNPs) is functionally essential during the eukaryotic process of

A. Mitochondrial electron transport
B. Pre-mRNA splicing inside the nucleus
C. Active transport across the plasma membrane
D. Translation of structural lipids on ribosomes

snRNPs ("snurps") are specialized nucleoproteins that combine to build the spliceosome, the machinery that removes non-coding introns.

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54. The biochemical function of the protein component (apolipoprotein) within a lipoprotein particle is to

A. Act as an enzyme or a ligand for specific cell receptors
B. Synthesize cholesterol molecules directly from water
C. Dissolve completely to release fats into the stomach lumen
D. Form covalent cross-links with the DNA of target tissues

Apolipoproteins act as structural scaffolding, activate lipid-processing enzymes, and serve as cell-surface ligands for target tissue receptors.

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Phosphoproteins, like milk casein or egg vitellin, are generated when phosphate groups attach covalently to serine, threonine, or tyrosine.

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52. The primary consequence of an individual possessing mutated, non-functional LDL receptors on their cell surfaces is

A. Abnormally low levels of circulating blood lipids
B. Severe hypercholesterolemia and premature atherosclerosis
C. Accelerated entry of cholesterol into peripheral cells
D. Total cessation of hepatic cholesterol production

Without working receptors, cells cannot internalize LDL particles via receptor-mediated endocytosis, causing cholesterol to build up in the blood.

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51. The biochemical feature shared by both glycoproteins and glycolipids present on the outer leaflet of erythrocyte membranes is that both

A. Possess negative charges due to phosphate groups
B. Carry short, branched oligosaccharide chains exposed to the exterior
C. Are synthesized completely within the nuclear matrix
D. Can act as independent ATP-synthase complexes

Both classes contribute to the structural cell coat by projecting their hydrophilic branched sugar chains into the extracellular space.

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