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
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
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