Structure of a kinetic protein folding intermediate by equilibrium amide exchange

1997 ◽  
Vol 4 (10) ◽  
pp. 801-804 ◽  
Author(s):  
Laszlo L. P. Hosszu ◽  
C. Jeremy Craven ◽  
Martin J. Parker ◽  
Mark Lorch ◽  
James Spencer ◽  
...  

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.


Biochemistry ◽  
2013 ◽  
Vol 52 (34) ◽  
pp. 5780-5789 ◽  
Author(s):  
Julianne L. Kitevski-LeBlanc ◽  
Joshua Hoang ◽  
William Thach ◽  
Sacha Thierry Larda ◽  
R. Scott Prosser

2010 ◽  
Vol 107 (51) ◽  
pp. 22106-22110 ◽  
Author(s):  
H. Neuweiler ◽  
W. Banachewicz ◽  
A. R. Fersht

2018 ◽  
Vol 122 (49) ◽  
pp. 11792-11799 ◽  
Author(s):  
Cyril Charlier ◽  
Joseph M. Courtney ◽  
Philip Anfinrud ◽  
Ad Bax

Biochemistry ◽  
2003 ◽  
Vol 42 (43) ◽  
pp. 12461-12465 ◽  
Author(s):  
Hanqiao Feng ◽  
Jiro Takei ◽  
Rebecca Lipsitz ◽  
Nico Tjandra ◽  
Yawen Bai

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