Lecture 9 Flashcards

1
Q

Protein Stability

A
  • Electrostatic Forces: Ion-ion interactions
  • Van der waals forces between permanent and induced dipoles
  • H-bonds
  • Hydrophobic forces, most important type of force holding proteins together
  • Hydrophobic amino acids tend to be in core
  • Charged amino acids tend to be on surface
  • Uncharged polar amino acids usually on surface but can be in the interior
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2
Q

Protein Denaturation

A
  • Native structure is the biologically relevant 3D structure of a protein
  • Denaturation is disrupting the forces holding the native structure together
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3
Q

How to denature a protein

A
  • Heat
  • addition of organic substances to disrupt hydrophobic interactions
  • chaotropic agents, increase the solubility of nonpolar substances in water, disrupt hydrophobic interactions
  • Denatured proteins can refold frequently
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