Elucidation of the denatured structure of protein in equilibrium with the native one under a physiological condition.

我们用核磁共振和H/D交换方法研究了溶菌酶的非结构二硫键缺陷变体中剩余的偏序结构。在这个残基结构中，α-折叠底部的两个残基I55和L56位于β-结构域的A、B和C-螺旋形成的疏水口袋中。溶菌酶折叠似乎是在这个位置附近开始的。另一方面，研究了吡咯烷酮羧基肽酶(PCP)在天然状态下的H/D交换反应。根据残基70附近的结构变化，发现天然结构分为两个结构域。

We have studied partially ordered structures remaining in unstructured disulfide-deficient variants of lysozyme by means of NMR and H/D exchange methods. In this residual structure, two residues of I55 and L56 involved in the bottom of the α-sheet were located in a hydrophobic pocket formed with A, B and C-helices in the β-domain. Lysozyme folding appears to be initiated around this site. On the other hand, H/D exchange reactions were studied in the native state of pyrrolidone carboxyl peptidase(PCP). The native structure was found to be divided into two domains by structural changes near at the residue 70.