Atomic force microscopy reveals the mechanical design of a modular protein

被引:242
作者
Li, HB
Oberhauser, AF
Fowler, SB
Clarke, J
Fernandez, JM [1 ]
机构
[1] Mayo Clin & Mayo Fdn, Dept Physiol & Biophys, Rochester, MN 55905 USA
[2] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England
关键词
D O I
10.1073/pnas.120048697
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
Tandem modular proteins underlie the elasticity of natural adhesives, cell adhesion proteins, and muscle proteins. The fundamental unit of elastic proteins is their individually folded modules. Here, we use protein engineering to construct multimodular proteins composed of Ig modules of different mechanical strength. We examine the mechanical properties of the resulting tandem modular proteins by using single protein atomic force microscopy. We show that by combining modules of known mechanical strength, we can generate proteins with novel elastic properties. Our experiments reveal the simple mechanical design of modular proteins and open the way for the engineering of elastic proteins with defined mechanical properties, which can be used in tissue and fiber engineering.
引用
收藏
页码:6527 / 6531
页数:5
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