title: Kinetic and equilibrium folding intermediates.
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.
authors.affiliation: Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region.
authors.forename: O B
authors.initials: OB
authors.lastname: Ptitsyn
authors.forename: V E
authors.initials: VE
authors.lastname: Bychkova
authors.forename: V N
authors.initials: VN
authors.lastname: Uversky
mesh_terms: D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D000432:Methanol; D011489:Protein Denaturation; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D000432:Methanol