Transcript Document

Protein folding reading:
Creighton sections 7.1, 7.3, 7.4 and 7.5
The nature of the unfolded state
Not completely random.
Molten globule state: Creighton pg 292
Denaturants:
Urea
Guanidinium Chloride
Temperature
pH
Other solvents
Most common chemical denaturants used
in protein folding studies
Effects of additives to protein solutions
Effects of some organic solvents
Increase solubility of polar and nonpolar side chains
Effects of the
counter anion
Absorbance
Aromatic amino acid residues absorb strongly
Folding
transitions
Transverse urea gradient electrophoresis
Can obtain DG directly from the data
Thermal denaturation
Need to obtain T* and DH*
DG for
different
proteins
Cooperative
versus
noncooperative
folding
Simulated Sequential mechanism: U -> I1 -> I2 -> N
Linked functions
The folding pathway for BPTI