The N-terminal to C-terminal motif in protein folding and function
The N-terminal to C-terminal motif in protein folding and function
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DOI：
10.1073/pnas.0409114102
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发表时间：
2005-01-25
影响因子：
11.1
通讯作者：
Englander, SW
中科院分区：
文献类型：
--
作者：
Krishna, MMG;Englander, SW
基本上所有已知以双态方式动力学折叠的蛋白质都具有接触的 N 端和 C 端二级结构元件，并且末端元件通常作为实验可测量的初始折叠步骤的一部分对接。相反，迄今为止研究的所有 N-C 非接触蛋白均通过非二态动力学折叠。相比之下，蛋白质数据库中大约一半的单域蛋白质的 N 端和 C 端元件相互接触，这超出了随机概率基础上的预期，但不足以解释蛋白质折叠的偏差。这种偏差的可能原因与初始蛋白质折叠、天然状态稳定性和最终周转的机制有关。
Essentially all proteins known to fold kinetically in a two-state manner have their N- and C-terminal secondary structural elements in contact, and the terminal elements often dock as part of the experimentally measurable initial folding step. Conversely, all N-C no-contact proteins studied so far fold by non-two-state kinetics. By comparison, about half of the single domain proteins in the Protein Data Bank have their N- and C-terminal elements in contact, more than expected on a random probability basis but not nearly enough to account for the bias in protein folding. Possible reasons for this bias relate to the mechanisms for initial protein folding, native state stability, and final turnover.