The study of protein mechanics with the atomic force microscope

被引：275

作者：

Fisher, TE ^{[1
]}

Oberhauser, AF ^{[1
]}

Carrion-Vazquez, M ^{[1
]}

Marszalek, PE ^{[1
]}

Fernandez, JM ^{[1
]}

机构：

[1] Mayo Clin & Mayo Fdn, Dept Physiol & Biophys, Rochester, MN 55905 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1999年 / 24卷 / 10期

关键词：

D O I：

10.1016/S0968-0004(99)01453-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The unfolding and folding of single protein molecules can be studied with an atomic force microscope (AFM). Many proteins with mechanical functions contain multiple, individually folded domains with similar structures. Protein engineering techniques have enabled the construction and expression of recombinant proteins that contain multiple copies of identical domains. Thus, the AFM in combination with protein engineering has enabled the kinetic analysis of the force-induced unfolding and refolding of individual domains as well as the study of the determinants of mechanical stability.

引用

页码：379 / 384

页数：6

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