Single molecule unzipping of coiled coils:: Sequence resolved stability profiles

被引：53

作者：

Bornschlögl, T ^{[1
]}

Rief, M ^{[1
]}

机构：

[1] Tech Univ Munich, Phys Dept E22, D-85748 Munich, Germany

来源：

PHYSICAL REVIEW LETTERS | 2006年 / 96卷 / 11期

关键词：

D O I：

10.1103/PhysRevLett.96.118102

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

We use a high resolution atomic force microscopy technique to mechanically unzip and rezip single coiled-coil proteins. This allows us to read off the complete stability profile of the protein turn by turn. We investigated three coiled coils with different length as well as a point mutation and find force fluctuations between 9 and 15 pN that can be directly related to the amino-acid sequences. An equilibrium model previously applied to DNA fully describes the mechanical unzipping process including free-energy contributions of the individual turns and seed formation energy.

引用

页数：4

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