Englander S Walter, Mayne Leland, Rumbley Jon N
Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA.
Biophys Chem. 2002 Dec 10;101-102:57-65. doi: 10.1016/s0301-4622(02)00190-4.
Hydrogen exchange experiments show that cytochrome c and other proteins under native conditions reversibly unfold in a multi-step manner. The step from one intermediate to the next is determined by the intrinsically cooperative nature of secondary structural elements, which is retained in the native protein. Folding uses the same pathway in the reverse direction, moving from the unfolded to the native state through relatively discrete intermediate forms by the sequential addition of native-like secondary structural units.
氢交换实验表明，细胞色素c和其他蛋白质在天然条件下以多步方式可逆地展开。从一个中间体到下一个中间体的步骤由二级结构元件的内在协同性质决定，这种性质在天然蛋白质中得以保留。折叠过程则沿相反方向使用相同的途径，通过依次添加类似天然的二级结构单元，从展开状态通过相对离散的中间体形式转变为天然状态。
