α-螺旋在C端比在N端折叠得更快。
The alpha-helix folds more rapidly at the C-terminus than at the N-terminus.
作者信息
Pozo Ramajo Angela, Petty Sarah A, Starzyk Agnieszka, Decatur Sean M, Volk Martin
机构信息
Department of Chemistry and Surface Science Research Centre, University of Liverpool, Liverpool L69 3BX, UK.
出版信息
J Am Chem Soc. 2005 Oct 12;127(40):13784-5. doi: 10.1021/ja054500+.
PMID:16201787
Abstract
The helix-coil dynamics of different sections of an alpha-helical model peptide were observed separately by nanosecond temperature jump experiments with IR detection on a series of isotopically labeled peptides. The results show that the helix-coil dynamics of the alpha-helical C-terminus are faster than those of the N-terminus.
摘要
通过对一系列同位素标记的肽进行红外检测的纳秒级温度跳跃实验，分别观察了α-螺旋模型肽不同区段的螺旋-卷曲动力学。结果表明，α-螺旋C末端的螺旋-卷曲动力学比N末端的更快。
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