Biologically active templates MCQs With Answer

Introduction

Biologically active templates are vital tools in modern protein science and pharmaceutical formulation. This blog presents focused MCQs to help M.Pharm students understand how templates—ranging from peptide fragments and nucleic acids to inorganic scaffolds and virus-like particles—guide protein folding, assembly, crystallization, and functionalization. Questions emphasize mechanism, analytical characterization, formulation advantages, and practical limitations such as immunogenicity and template removal. Designed for revision and exam preparation, the set advances beyond definitions into applied concepts like epitope imprinting, templated self-assembly, seeded aggregation, and protein-templated synthesis. Each question includes plausible distractors and concise answers to reinforce deep conceptual understanding relevant to drug development and protein formulations.

Q1. Which statement best defines a biologically active template in the context of protein science?

• Any polymer used to encapsulate proteins for delivery
• Molecules that direct the assembly, folding or synthesis of biomolecules, producing a specific biological activity
• A chemical cross-linker used to stabilize tertiary structure
• An inert surface used only for analytical separation

Correct Answer: Molecules that direct the assembly, folding or synthesis of biomolecules, producing a specific biological activity

Q2. Template-assisted protein folding typically relies on which primary mechanism?

• Formation of permanent covalent bonds between template and substrate
• Provision of a sequence-specific genetic code
• Guidance by non-covalent interactions and spatial constraints from a pre-existing scaffold
• Random collisions in high ionic strength buffers

Correct Answer: Guidance by non-covalent interactions and spatial constraints from a pre-existing scaffold

Q3. In molecular imprinting for protein recognition, what advantage does epitope imprinting have over imprinting the entire protein?

• Requires larger template amounts and longer polymerization times
• Yields binding sites specific to a short, exposed peptide region, improving selectivity and template removal
• Creates non-specific hydrophobic cavities that bind many proteins
• Generates irreversible covalent bonds with the target protein

Correct Answer: Yields binding sites specific to a short, exposed peptide region, improving selectivity and template removal

Q4. Which driving forces most commonly mediate templated self-assembly of protein nanostructures?

• High-energy covalent cross-linking only
• Non-covalent interactions such as hydrogen bonding, hydrophobic interactions and electrostatic complementarity
• Radiation-induced polymerization
• Extreme pH causing irreversible denaturation

Correct Answer: Non-covalent interactions such as hydrogen bonding, hydrophobic interactions and electrostatic complementarity

Q5. What is a major formulation benefit of using templates during protein crystallization?

• Elimination of all solvent molecules from the crystal lattice
• Control over nucleation leading to improved crystal quality and potentially selective polymorph formation
• Guaranteed prevention of any aggregation during storage
• Conversion of proteins into purely amorphous solids

Correct Answer: Control over nucleation leading to improved crystal quality and potentially selective polymorph formation

Q6. In the context of amyloid formation, what does “templated seeding” refer to?

• Thermal degradation of fibrils to monomers
• Heterogeneous nucleation where pre-formed fibril fragments act as seeds to accelerate fibril growth from monomers
• Spontaneous formation of fibrils without any seeds
• Use of chemical cross-linkers to prevent fibrillation

Correct Answer: Heterogeneous nucleation where pre-formed fibril fragments act as seeds to accelerate fibril growth from monomers

Q7. Virus-like particles (VLPs) are an example of which templating strategy in vaccine design?

• Enzymatic cleavage templates
• Proteinaceous templates that mimic viral capsid architecture to present antigens in a repetitive array
• Inorganic silica templates for thermal stabilization
• Small-molecule templates that covalently bond to antigens

Correct Answer: Proteinaceous templates that mimic viral capsid architecture to present antigens in a repetitive array

Q8. Which reaction best exemplifies protein-templated chemical synthesis in drug discovery?

• Random polymerization of acrylates in solution
• Proximity-driven ligation of two fragments only when both bind adjacent sites on a protein surface
• High temperature pyrolysis of peptides
• Non-selective oxidation of all accessible thiols

Correct Answer: Proximity-driven ligation of two fragments only when both bind adjacent sites on a protein surface

Q9. Which analytical technique provides direct visualization of templated nanostructures formed by proteins?

• UV–Vis spectroscopy
• Transmission electron microscopy (TEM)
• High-performance liquid chromatography (HPLC) retention time
• Colorimetric pH indicators

Correct Answer: Transmission electron microscopy (TEM)

Q10. What is a common method for removing template molecules after polymer formation in a molecularly imprinted polymer for proteins?

• High-energy gamma irradiation
• Solvent extraction often combined with enzymatic or chemical cleavage for peptide/protein templates
• Immediate heating to 300 °C to decompose the template
• Permanent covalent trapping of the template to increase selectivity

Correct Answer: Solvent extraction often combined with enzymatic or chemical cleavage for peptide/protein templates

Q11. How can biologically active templates improve specificity in targeted protein delivery systems?

• By increasing non-specific adsorption to all cell types
• By providing molecular recognition elements that selectively bind target receptors and control release kinetics
• By permanently denaturing the payload protein to slow release
• By preventing any interaction with biological membranes

Correct Answer: By providing molecular recognition elements that selectively bind target receptors and control release kinetics

Q12. Which of the following is a significant limitation when using biological templates in formulations?

• Templates are always completely inert and never affect immunogenicity
• Potential for immunogenic response or toxicity if the template is not biocompatible or not fully removed
• Templates guarantee permanent stabilization of any protein under all conditions
• Templates eliminate the need for analytical characterization

Correct Answer: Potential for immunogenic response or toxicity if the template is not biocompatible or not fully removed

Q13. What feature of epitope-imprinted polymers often yields higher affinity for the native protein in complex mixtures?

• Creation of large, non-specific cavities that trap many macromolecules
• Formation of binding sites complementary to an exposed linear peptide sequence of the target
• Use of irreversible covalent cross-links that denature target proteins
• Embedding of metal ions that bind any protein indiscriminately

Correct Answer: Formation of binding sites complementary to an exposed linear peptide sequence of the target

Q14. In the endoplasmic reticulum quality-control, how do N-linked glycans function as templates?

• They form permanent covalent attachments to misfolded domains
• Glycan structures are recognized by lectin chaperones and serve as folding/quality-control signals guiding correct folding
• They always prevent any conformational change during folding
• Glycans cause immediate proteolytic degradation of newly synthesized proteins

Correct Answer: Glycan structures are recognized by lectin chaperones and serve as folding/quality-control signals guiding correct folding

Q15. Which biomolecule class is the canonical example of acting as an information-bearing template for sequence-specific polymerization?

• Lipids in bilayers
• Nucleic acids (DNA/RNA) serving as templates for complementary polymerization
• Polysaccharides that randomly polymerize monomers
• Simple salts forming ionic lattices

Correct Answer: Nucleic acids (DNA/RNA) serving as templates for complementary polymerization

Q16. What is the primary role of an inorganic template such as silica in forming protein-based nanocages?

• Introduce covalent cross-links that denature proteins
• Provide a rigid scaffold that directs protein arrangement into defined architectures and sizes
• Ensure complete solubilization of hydrophobic proteins in water
• Eliminate the need for buffering agents

Correct Answer: Provide a rigid scaffold that directs protein arrangement into defined architectures and sizes

Q17. How do chaperonins (e.g., GroEL/GroES) primarily assist protein folding compared to a simple template surface?

• They act solely by covalently modifying substrates
• They provide an isolated, ATP-driven chamber that prevents aggregation and allows productive folding cycles rather than a static template
• They hydrolyze the amino acids of unfolded proteins
• They permanently bind and sequester misfolded proteins for degradation

Correct Answer: They provide an isolated, ATP-driven chamber that prevents aggregation and allows productive folding cycles rather than a static template

Q18. Which biophysical method is best suited to quantify binding kinetics between a template and a protein in real time?

• Solid-phase microextraction
• Surface plasmon resonance (SPR)
• Gel electrophoresis mobility shift without kinetic data
• Simple thin-layer chromatography

Correct Answer: Surface plasmon resonance (SPR)

Q19. Cross-seeding between different amyloidogenic proteins is most likely when:

• The sequences have no structural similarity
• Short segments share β-sheet-prone motifs or complementary structural templates enabling heterologous nucleation
• Proteins are fully glycosylated and folded correctly
• One protein is entirely hydrophilic and highly disordered with no β-prone sequence

Correct Answer: Short segments share β-sheet-prone motifs or complementary structural templates enabling heterologous nucleation

Q20. When designing biologically active templates for formulation use, which considerations are most critical?

• Only the visual color of the template matters
• Template biocompatibility, ease of removal or biodegradability, influence on target stability, and minimization of immunogenicity
• Ensuring the template permanently binds irreversibly to all formulation components
• Maximizing template hydrophobicity at the expense of protein activity

Correct Answer: Template biocompatibility, ease of removal or biodegradability, influence on target stability, and minimization of immunogenicity

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