Kinetic and equilibrium folding intermediates
1995 ◽
Vol 348
(1323)
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pp. 35-41
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Keyword(s):
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.
2007 ◽
Vol 68
(3)
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pp. 606-616
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Keyword(s):
1993 ◽
Vol 58
(7)
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pp. 1624-1630
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Keyword(s):
Keyword(s):
2014 ◽
Vol 111
(41)
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pp. 14746-14751
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Keyword(s):
1999 ◽
Vol 146
(10)
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pp. 3802-3806
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Keyword(s):
2019 ◽
Vol 126
◽
pp. 1288-1294
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Keyword(s):