scholarly journals The molten globule state as an intermediate of protein folding.

1993 ◽  
Vol 33 (1) ◽  
pp. 26-30
Author(s):  
Kunihiro KUWAJIMA

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.


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

Biochemistry ◽  
1993 ◽  
Vol 32 (48) ◽  
pp. 13198-13203 ◽  
Author(s):  
Akio Shimizu ◽  
Masamichi Ikeguchi ◽  
Shintaro Sugai

1996 ◽  
Vol 257 (4) ◽  
pp. 877-885 ◽  
Author(s):  
Christian Rischel ◽  
Per Thyberg ◽  
Rudolf Rigler ◽  
Flemming M. Poulsen

1996 ◽  
Vol 10 (1) ◽  
pp. 102-109 ◽  
Author(s):  
Kunihiro Kuwajima

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