Stepwise unfolding of ankyrin repeats in a single protein revealed by atomic force microscopy

被引:65
作者
Li, LW
Wetzel, S
Plückthun, A
Fernandez, JM [1 ]
机构
[1] Columbia Univ, Dept Biol Sci, New York, NY 10027 USA
[2] Univ Zurich, Inst Biochem, CH-8057 Zurich, Switzerland
关键词
D O I
10.1529/biophysj.105.078436
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Using single-molecule atomic force microscopy, we find that a protein consisting of six identical ankyrin repeat units flanked by N- and C- terminal modules (N6C) unfolds in a stepwise, unit-by-unit fashion under a mechanical force. Stretching a N6C molecule results in a sawtooth pattern fingerprint, with as many as six peaks separated by similar to 10 nm and an average unfolding force of 50 +/- 20 pN. Our results demonstrate that a stretching force can unfold multiple repeat units individually in a single protein molecule, despite extensive hydrophobic interactions between adjacent units.
引用
收藏
页码:L30 / L32
页数:3
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