Flashcards in Lecture 6- Protein Folding I Deck (14):
Describe the different types of non-covalent interactions:
VdW- charges (e-) fluctuate around an atom, forming temporary dipole moments
electrostatic- charges on one atom interact with charges on another, as described by Coulomb's law
hydrogen bonding- partial charges from hydrogen interact with Nitrogen and Oxygen
short range repulsion-
Protein folding is a highly (random/cooperative) process
Secondary structure plays an important part in the ____ of proteins.
The conformation of a protein is the result of specific _____.
How does hydrophobicity act as a determinant of folding?
Hydrophobic AAs tend to "cluster together" in pockets of hydrophobicity (usually found within the plasma membrane)
Draw/describe the steps of protein folding.
1) Secondary structure is rapidly achieved (high E* state)
2) Format'n of hydrophobic domains (cooperative) leading to "core protein"
3) Formation of a molten globule
4) Adjustment of structure to native, low E* structure
The dynamic conformational state between native protein and full-unfolded protein
Why is the concept of the "molten globule" important?
The molten globule exists as the protein tries to find a low E*, highly ordered, thermodynamically stable structure
What two major types of interactions determine protein folding?
Non-covalent and hydrophobic interactions
Describe the characteristics of the "molten globule"
1) Presence of some 2* "native structure" elements - the beginnings of final form are taking shape
2) No specific 3* structure - no packing of side chains
3) Compact into the overall shape of the protein, but radius is still 10-30% larger than final native protein's radius
4) Loosely packed hydrophobic core
Repeating secondary structure present in many proteins that exhibit similar f(x)s
Structural charachteristics of a protein (ex: repeated alpha-helices)
A specific functional region of a protein
domain (ex: antigen binding domain on an anti-body)