Kinetic and equilibrium folding intermediates

O u r recent experim ents on the m olten globule state and o ther protein folding in term ediates lead to following conclusions: (i) the m olten globule is separated by in tram olecular first-order phase transitions from the native and unfolded states and therefore is a specific therm odynam ic state of protein molecules; (ii) the novel equilibrium folding in term ediate (the ‘pre-m olten g lobu le’ state) exists which can be sim ilar to the ‘b u rs t’ kinetic in term ediate of protein folding; (iii) proteins denatu re and release their non-polar ligands a t m oderately low pH and m oderately low dielectric constant, i.e. under conditions which m ay be related to those near m em branes.