Kinetic and equilibrium folding intermediates
Philosophical Transactions of the Royal Society B Biological SciencesPublished 29 April 1995
Oleg B. Ptitsyn, Valentina E. Bychkova, Vladimir N. Uversky
Citations116
SJR quartileQ1
SJR score1.73
SNIP1.64
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TL;DR
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.
Abstract
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.
Keywords
Materials ScienceAgricultural and Biological SciencesBiochemistry, Genetics and Molecular Biology
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