Folding of the C-terminal fragment V111-D143 of staphylococcal nuclease in aqueous solution.
Folding of the C-terminal fragment V111-D143 of staphylococcal nuclease in aqueous solution.
复制标题
水溶液中葡萄球菌核酸酶 C 端片段 V111-D143 的折叠。
DOI：
10.2174/092986607781483769
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发表时间：
2007
期刊：
影响因子：
--
通讯作者：
Jinfeng Wang
中科院分区：
文献类型：
--
作者：
Y. Geng;Min Wang;T. Xie;Yingang Feng;Jinfeng Wang
SNase（111-143）和SNase（118-143）片段及1-139片段中E122-K136片段构象特征的研究（SNase 139）表明，只有当片段V111-H121和L137-D143侧接在片段E122-K136上时，高的内在螺旋倾向才能驱动片段E122-K136折叠成稳定的螺旋。K136在葡萄球菌核酸酶（SNase）中具有稳定的折叠。
Studies of conformational features of fragments SNase(111-143) and SNase(118-143) and segment E122-K136 in 1-139 fragment (SNase139) suggest that the high intrinsic helical propensity can drive segment E122-K136 fold into a stable helix only when the segments V111-H121 and L137-D143 flanked on segment E122-K136 in staphylococcal nuclease (SNase) have stable folding.