Kutyshenko V P, Prokhorov D A
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Oblast, 142290 Russia.
Mol Biol (Mosk). 2003 Nov-Dec;37(6):1055-60.
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.
利用高分辨率核磁共振波谱研究了盐酸胍诱导的碳酸酐酶熔球态的去折叠过程。该研究估算了溶液中不同变性剂浓度下与熔球态结合的水分子和变性剂分子的数量。与天然碳酸酐酶去折叠的数据相比，这些估算结果表明，去折叠的基础是蛋白质分子附近变性剂局部浓度的增加，这是由盐酸胍结合水与蛋白质结合水的比例增加所致。
