[Guanidine hydrochloride mediated unfolding of a carbonic anhydrase molten globule].
Guanidine hydrochloride-induced unfolding of a carbonic anhydrase molten globule was studied by high-resolution NMR spectroscopy. The study resulted in estimation of the number of water and denaturant molecules bound to the molten globule at various denaturant concentrations in solution. When compared with the data on unfolding of native carbonic anhydrase, these estimates indicate that the unfolding is underlain by an increased local concentration of the denaturant near the protein molecule, which results from the increased ratio between guanidine hydrochloride-bound and protein-bound waters.
Kutyshenko
V P
VP
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Oblast, 142290 Russia. kutyshenko@rambler.ru
Prokhorov
D A
DA
D002256:Carbonic Anhydrases / Q000737:chemistry*; D019791:Guanidine / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation
D002256:Carbonic Anhydrases; D019791:Guanidine