Comment on "Force-clamp spectroscopy monitors the folding trajectory of a single protein"

被引：20

作者：

Sosnick, TR ^{[1
]}

机构：

[1] Univ Chicago, Dept Biochem & Mol Biol, Chicago, IL 60637 USA

来源：

SCIENCE | 2004年 / 306卷 / 5695期

关键词：

D O I：

10.1126/science.1100962

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

In a recent report on atomic force microscopy (AFM)-monitored protein folding, Fernandez and Li (Reports, 12 March 2004, p. 1674) concluded that the folding of the single-domain protein ubiquitin does not correspond to transitions between discrete states. The results are inconsistent with solution studies of ubiquitin folding and probably are due in part to chain-tangling in the tethered polyprotein construct used in the AFM studies.

引用

页码：411B / +

页数：2

共 17 条

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