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.
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页码：411B / +
页数：2
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