Understanding the biological role of proteins is essential for B. Pharm students preparing for pharmacology, biochemistry, and therapeutics. This concise guide introduces protein functions—enzymes, structural proteins, transporters, signaling molecules, immunoglobulins, and peptide hormones—highlighting relevance to drug action, metabolism, and disease. Focused on mechanisms such as enzyme catalysis, receptor binding, membrane transport, and post-translational modifications, these MCQs with answers reinforce core concepts, clinical correlations, and exam-ready facts. Keywords include Biological role of proteins MCQs With Answer, B.Pharm, protein functions, enzymes in drug metabolism, and protein structure-function relationships, and practical applications. Now let’s test your knowledge with 50 MCQs on this topic.
Q1. Which bond links amino acids together to form the primary structure of proteins?
- Hydrogen bond
- Peptide bond
- Disulfide bond
- Ionic bond
Correct Answer: Peptide bond
Q2. Which level of protein structure is primarily stabilized by hydrogen bonding between backbone NH and CO groups?
- Primary structure
- Secondary structure
- Tertiary structure
- Quaternary structure
Correct Answer: Secondary structure
Q3. Which amino acid is unique for introducing kinks in alpha helices due to its cyclic structure?
- Glycine
- Proline
- Alanine
- Serine
Correct Answer: Proline
Q4. Which protein is the major carrier of fatty acids and many drugs in plasma, influencing drug distribution?
- Hemoglobin
- Albumin
- Fibrinogen
- Transferrin
Correct Answer: Albumin
Q5. Enzymes accelerate reactions primarily by
- Increasing activation energy
- Decreasing activation energy
- Changing the equilibrium constant
- Altering substrate concentration
Correct Answer: Decreasing activation energy
Q6. The Michaelis constant (Km) represents
- The maximum reaction rate
- The substrate concentration at half Vmax
- The affinity between enzyme and inhibitor
- The turnover number
Correct Answer: The substrate concentration at half Vmax
Q7. A competitive inhibitor affects enzyme kinetics by
- Decreasing Vmax and increasing Km
- Increasing Vmax and decreasing Km
- Increasing Km without changing Vmax
- Decreasing Km without changing Vmax
Correct Answer: Increasing Km without changing Vmax
Q8. Allosteric enzymes often display which type of kinetic behavior?
- Linear kinetics
- Michaelis-Menten hyperbolic curve
- Sigmoidal (cooperative) kinetics
- First-order kinetics only
Correct Answer: Sigmoidal (cooperative) kinetics
Q9. Which protein is responsible for oxygen transport in red blood cells and shows cooperative binding?
- Myoglobin
- Albumin
- Hemoglobin
- Collagen
Correct Answer: Hemoglobin
Q10. Myoglobin differs from hemoglobin mainly because it
- Is a tetramer and shows cooperativity
- Binds CO2 preferentially
- Is a monomer and stores oxygen in muscle
- Is a membrane receptor
Correct Answer: Is a monomer and stores oxygen in muscle
Q11. Which post-translational modification commonly regulates enzyme activity and signal transduction?
- Glycolysis
- Phosphorylation
- Proteasomal degradation
- Transcription
Correct Answer: Phosphorylation
Q12. Protein glycosylation is important for
- DNA replication fidelity
- Membrane receptor recognition and stability
- RNA splicing
- ATP synthesis in mitochondria
Correct Answer: Membrane receptor recognition and stability
Q13. Which class of proteins includes antibodies essential for adaptive immunity?
- Enzymes
- Immunoglobulins
- Transporters
- Structural proteins
Correct Answer: Immunoglobulins
Q14. Zymogens are
- Inactive enzyme precursors activated by proteolysis
- Allosteric activators of enzymes
- Membrane-bound receptors
- Chaperone proteins
Correct Answer: Inactive enzyme precursors activated by proteolysis
Q15. Which degradation pathway labels proteins with ubiquitin for proteasomal destruction?
- Lysosomal autophagy
- Ubiquitin-proteasome system
- Glycolytic pathway
- ER secretory pathway
Correct Answer: Ubiquitin-proteasome system
Q16. Heat shock proteins (molecular chaperones) primarily function to
- Degrade misfolded proteins
- Assist proper protein folding and prevent aggregation
- Synthesize proteins on ribosomes
- Transport proteins across membranes
Correct Answer: Assist proper protein folding and prevent aggregation
Q17. Which amino acid contains a thiol group that forms disulfide bonds important for tertiary structure?
- Methionine
- Cysteine
- Tyrosine
- Serine
Correct Answer: Cysteine
Q18. Prion diseases result from proteins that
- Are overphosphorylated
- Adopt an infectious misfolded conformation that induces aggregation
- Have increased enzymatic activity
- Are secreted at excessive levels
Correct Answer: Adopt an infectious misfolded conformation that induces aggregation
Q19. Which plasma protein is essential for blood clot formation by being converted to fibrin?
- Albumin
- Fibrinogen
- Transferrin
- Globin
Correct Answer: Fibrinogen
Q20. Cytochrome P450 enzymes are important in drug metabolism because they
- Conjugate drugs directly to glucuronic acid
- Oxidize xenobiotics, increasing polarity for excretion
- Transport drugs across the BBB
- Act as membrane ion channels
Correct Answer: Oxidize xenobiotics, increasing polarity for excretion
Q21. Which structural protein provides tensile strength to connective tissues and is abundant in bone and skin?
- Actin
- Keratin
- Collagen
- Tubulin
Correct Answer: Collagen
Q22. The quaternary structure of a protein refers to
- The amino acid sequence
- Local folding patterns like alpha helices
- Three-dimensional folding of a single polypeptide
- The assembly of multiple polypeptide subunits
Correct Answer: The assembly of multiple polypeptide subunits
Q23. Which protein domain is typically responsible for binding small ligands like cofactors or drugs?
- Signal peptide
- Active site or binding pocket
- Transmembrane helix
- Coiled-coil domain
Correct Answer: Active site or binding pocket
Q24. Which cellular compartment is the primary site for secretory and membrane protein folding and glycosylation?
- Nucleus
- Endoplasmic reticulum
- Mitochondria
- Cytosol
Correct Answer: Endoplasmic reticulum
Q25. Which receptor type has intrinsic tyrosine kinase activity and mediates many growth factor signals?
- G protein-coupled receptor (GPCR)
- Ion channel receptor
- Toll-like receptor
- Receptor tyrosine kinase (RTK)
Correct Answer: Receptor tyrosine kinase (RTK)
Q26. Insulin is classified as which type of biomolecule?
- Steroid hormone
- Peptide hormone (protein)
- Neurotransmitter
- Fatty acid derivative
Correct Answer: Peptide hormone (protein)
Q27. Which component determines the specificity of antibody binding to antigen?
- Fc region
- Hinge region
- Variable region (Fab)
- Constant region
Correct Answer: Variable region (Fab)
Q28. Which laboratory technique separates proteins primarily by molecular weight under denaturing conditions?
- Isoelectric focusing
- SDS-PAGE
- Native PAGE
- Affinity chromatography
Correct Answer: SDS-PAGE
Q29. Enzyme turnover number (kcat) represents
- The substrate concentration at half Vmax
- The number of substrate molecules converted per enzyme per unit time
- The binding affinity of enzyme for substrate
- The inhibitor potency
Correct Answer: The number of substrate molecules converted per enzyme per unit time
Q30. Hemoglobin affinity for oxygen decreases under conditions of
- Low CO2, high pH
- High pH and low temperature
- High CO2, low pH, and high 2,3-BPG
- Presence of methemoglobin only
Correct Answer: High CO2, low pH, and high 2,3-BPG
Q31. Which modification targets proteins for lysosomal degradation via mannose-6-phosphate tagging?
- Ubiquitination
- N-linked glycosylation with Mannose-6-phosphate
- Phosphorylation
- Acetylation
Correct Answer: N-linked glycosylation with Mannose-6-phosphate
Q32. Which protein family forms the cytoskeletal tracks used by motor proteins like kinesin and dynein?
- Actin filaments
- Intermediate filaments
- Microtubules (tubulin)
- Collagen fibrils
Correct Answer: Microtubules (tubulin)
Q33. Which technique would you use to quantify a specific protein in patient serum using antigen-antibody specificity?
- Western blot
- ELISA
- Mass spectrometry
- Spectrophotometry
Correct Answer: ELISA
Q34. The term “isoenzyme” refers to
- Different enzymes performing different reactions
- Different molecular forms of the same enzyme catalyzing the same reaction
- Inactive enzyme precursors
- Enzymes bound to membranes only
Correct Answer: Different molecular forms of the same enzyme catalyzing the same reaction
Q35. Which protein modification commonly increases protein half-life by blocking degradation signals?
- Polyubiquitination
- N-terminal acetylation
- Proteolytic cleavage
- Dephosphorylation
Correct Answer: N-terminal acetylation
Q36. Which protein acts as a molecular oxygen sensor in some regulatory pathways by binding heme and modulating activity?
- Hemoglobin only
- HIF (hypoxia-inducible factor) regulated proteins
- Cytochrome P450 family member exclusively
- Albumin
Correct Answer: HIF (hypoxia-inducible factor) regulated proteins
Q37. Which drug class often inhibits proteases and is used in antiviral therapy?
- Beta-lactam antibiotics
- Protease inhibitors
- Calcium channel blockers
- Statins
Correct Answer: Protease inhibitors
Q38. Which term describes the non-protein component required for enzyme activity?
- Apoenzyme
- Coenzyme or prosthetic group
- Substrate
- Inhibitor
Correct Answer: Coenzyme or prosthetic group
Q39. Which membrane protein type spans the lipid bilayer and often forms channels or receptors?
- Peripheral proteins
- Lipoproteins
- Integral (transmembrane) proteins
- Glycolytic enzymes
Correct Answer: Integral (transmembrane) proteins
Q40. Protein misfolding leading to amyloid fibrils is characteristic of which condition?
- Type I hypersensitivity
- Amyloidosis and neurodegenerative diseases like Alzheimer’s
- Acute bacterial infection only
- Vitamin deficiency syndromes
Correct Answer: Amyloidosis and neurodegenerative diseases like Alzheimer’s
Q41. Coagulation factors are mostly which type of biomolecule?
- Carbohydrates
- Lipids
- Proteins (serine proteases or glycoproteins)
- Steroid hormones
Correct Answer: Proteins (serine proteases or glycoproteins)
Q42. Which amino acid is commonly phosphorylated to regulate protein activity in signaling pathways?
- Phenylalanine
- Tyrosine, serine, or threonine
- Leucine
- Proline only
Correct Answer: Tyrosine, serine, or threonine
Q43. Which proteomic technique separates proteins based on isoelectric point and molecular weight?
- Two-dimensional gel electrophoresis (2D-PAGE)
- SDS-PAGE only
- ELISA
- PCR
Correct Answer: Two-dimensional gel electrophoresis (2D-PAGE)
Q44. Which protein is central to innate immunity by recognizing pathogen-associated molecular patterns?
- Immunoglobulin G (IgG)
- Toll-like receptors (TLRs)
- Albumin
- Insulin
Correct Answer: Toll-like receptors (TLRs)
Q45. Which property of amino acids determines whether a protein is soluble in water?
- Primary sequence length only
- Proportion and distribution of hydrophobic vs hydrophilic residues
- Number of disulfide bonds only
- Presence of metal ions only
Correct Answer: Proportion and distribution of hydrophobic vs hydrophilic residues
Q46. Signal peptides at the N-terminus of proteins direct them to the
- Mitochondrial matrix only
- Secretory pathway (ER) for secretion or membrane insertion
- Nucleus exclusively
- Peroxisomes only
Correct Answer: Secretory pathway (ER) for secretion or membrane insertion
Q47. Which laboratory assay measures enzyme activity by monitoring product formation over time?
- Western blot
- Enzyme activity assay (kinetic assay)
- Immunoprecipitation
- Southern blot
Correct Answer: Enzyme activity assay (kinetic assay)
Q48. Which pharmacological strategy uses monoclonal antibodies to target specific proteins involved in disease?
- Small-molecule inhibitors only
- Monoclonal antibody therapy
- Gene editing exclusively
- Vaccine adjuvants only
Correct Answer: Monoclonal antibody therapy
Q49. The Hill coefficient greater than 1 for a protein indicates
- Negative cooperativity
- No cooperativity
- Positive cooperativity among binding sites
- Complete inhibition of binding
Correct Answer: Positive cooperativity among binding sites
Q50. In the context of drug development, why is understanding protein structure-function relationships vital?
- It is only academically interesting with no practical use
- It informs rational drug design, target validation, and predicting off-target effects
- It replaces the need for clinical trials
- It is only relevant for nutritional studies
Correct Answer: It informs rational drug design, target validation, and predicting off-target effects

I am a Registered Pharmacist under the Pharmacy Act, 1948, and the founder of PharmacyFreak.com. I hold a Bachelor of Pharmacy degree from Rungta College of Pharmaceutical Science and Research. With a strong academic foundation and practical knowledge, I am committed to providing accurate, easy-to-understand content to support pharmacy students and professionals. My aim is to make complex pharmaceutical concepts accessible and useful for real-world application.
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