DTU BIO3 exam questions

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13 Terms

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Favourable and Unfavourable Interactions in Protein Folding

  • Favourable Interactions: Hydrophobic effect, hydrogen bonding, van der Waals forces.

  • Unfavourable Interactions: Chain conformational entropy

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What are Intrinsically Disordered Proteins?

Proteins that lack a fixed or ordered three-dimensional structure

 

Involved in cell signaling, transcription, and chromatin remodeling

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What are examples of Protein Misfolding/Aggregation Diseases?

Alzheimer's disease, Parkinson's disease, cystic fibrosis

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What is Allostery?

Regulation of a protein's activity through binding at a site other than the active site, causing a conformational change

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What is the difference between enzymes and Non-Biological Catalysts?

 

  • Enzymes: Highly specific, operate under mild conditions, biodegradable

 

  • Non-Biological Catalysts: Less specific, can operate under extreme conditions, not biodegradable

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What is Directed Evolution?

Mimicking natural selection in the lab to improve enzyme functions

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What are antibodies?

Proteins that bind to antigens to neutralize pathogens

 

  • Applications: Diagnostics, passive immunity, autoimmune disease treatment

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What is the advantage of nanobodies compared to classical antibodies?

Smaller, better tissue penetration, easier production. Stability under extreme conditions, high antigen-binding affinity

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What is Protein Display Technologies (Phage Display)?

  • Expressing peptide or protein sequences on bacteriophages to identify ligands

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What is the concept of proteomics?

  • Large-scale study of proteins, their structures, interactions, and functions, used for mass spectrometry

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What are the advantages and disadvantages of chemical synthesis and recombinant production of proteins?

 

  • Advantages: Chemical synthesis allows precise control over protein modifications; recombinant production is cost-effective for large quantities.

  • Disadvantages: Chemical synthesis can be expensive and complex; recombinant production may have issues with protein folding and post-translational modifications.

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What is self-assembly in biology?

  • Process where molecules spontaneously form organized structures, for example formation of lipid bilayers and protein complexes.

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What are examples of food protein sources?

  • Plant-based proteins (e.g., soy, pea), insect proteins, lab-grown meat.