Kobayashi N, Honda S, Yoshii H, Uedaira H, Munekata E
Institute of Applied Biochemistry, University of Tsukuba, Japan.
FEBS Lett. 1995 Jun 12;366(2-3):99-103. doi: 10.1016/0014-5793(95)00503-2.
We examined the complementation of various pairs of fragments derived from the streptococcal protein G B1 domain by NMR and CD. Most were not associated; however, one pair of fragments (1-40) and (41-56) interacted sufficiently enough to regenerated a stable 1:1 complex, Kd = 9 x 10(-6) M. A 2D-NMR analysis showed that the structure of the complex resembled that of native domain. Here we discuss the complementation from the viewpoint of the folding pathway of the protein.
我们通过核磁共振（NMR）和圆二色光谱（CD）研究了源自链球菌蛋白G B1结构域的各对片段的互补作用。大多数片段没有相互作用；然而，一对片段（1 - 40）和（41 - 56）相互作用足够强，足以再生出稳定的1:1复合物，解离常数（Kd）= 9×10⁻⁶ M。二维核磁共振分析表明，该复合物的结构类似于天然结构域。在此，我们从蛋白质折叠途径的角度讨论这种互补作用。
