Kinetic and Equilibrium Folding Intermediates
Document Type
Article
Publication Date
1995
Digital Object Identifier (DOI)
https://doi.org/10.1098/rstb.1995.0043
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.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
The Royal Society, v. 348, issue 1323
Scholar Commons Citation
Ptitsyn, Oleg B.; Bychkova, Valentina E.; and Uversky, Vladimir N., "Kinetic and Equilibrium Folding Intermediates" (1995). Molecular Medicine Faculty Publications. 631.
https://digitalcommons.usf.edu/mme_facpub/631
