Role of the molten globule state in protein folding

2000 ◽  
pp. 209-282 ◽  
Author(s):  
Munehito Arai ◽  
Kunihiro Kuwajima
Keyword(s):  
Protein Folding ◽  
Molten Globule ◽  
Molten Globule State

Kinetic and equilibrium folding intermediates

1995 ◽  
Vol 348 (1323) ◽  
pp. 35-41 ◽  
Keyword(s):  
Protein Folding ◽  
Molten Globule ◽  
Low Dielectric Constant ◽  
The Novel ◽  
Folding Intermediate ◽  
Molten Globule State ◽  
Folding Intermediates ◽  
First Order ◽  
Low Dielectric ◽  
First Order Phase

Our recent experiments on the molten globule state and other protein folding intermediates lead to following conclusions: (i) the molten globule is separated by intramolecular first-order phase transitions from the native and unfolded states and therefore is a specific thermodynamic state of protein molecules; (ii) the novel equilibrium folding intermediate (the ‘pre-molten globule’ state) exists which can be similar to the ‘burst’ kinetic intermediate of protein folding; (iii) proteins denature and release their non-polar ligands at moderately low pH and moderately low dielectric constant, i.e. under conditions which may be related to those near membranes.

scholarly journals Evidence for a molten globule state as a general intermediate in protein folding

FEBS Letters ◽  
1990 ◽  
Vol 262 (1) ◽  
pp. 20-24 ◽  
Author(s):  
O.B. Ptitsyn ◽  
R.H. Pain ◽  
G.V. Semisotnov ◽  
E. Zerovnik ◽  
O.I. Razgulyaev
Keyword(s):  
Protein Folding ◽  
Molten Globule ◽  
Molten Globule State
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