AFM of biological complexes: What can we learn?

被引:40
作者
Gaczynska, Maria [1 ]
Osmulski, Pawel A. [1 ]
机构
[1] Univ Texas Hlth Sci Ctr San Antonio, Inst Biotechnol, Dept Mol Med, San Antonio, TX 78245 USA
关键词
atomic force microscopy; protein complexes; protein structure; allostery; proteasome; GroEL; amyloid; nanomedicine;
D O I
10.1016/j.cocis.2008.01.004
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The term "biological complexes" broadly encompasses particles as diverse as multisubunit enzymes, viral capsids, transport cages, molecular nets, ribosomes, nucleosomes, biological membrane components and amyloids. The complexes represent a broad range of stability and composition. Atomic force microscopy offers a wealth of structural and functional data about such assemblies. For this review, we choose to comment on the significance of AFM to study various aspects of biology of selected non-membrane protein assemblies. Such particles are large enough to reveal many structural details under the AFM probe. Importantly, the specific advantages of the method allow for gathering dynamic information about their formation, stability or allosteric structural changes critical for their function. Some of them have already found their way to nanomedical or nanotechnological applications. Here we present examples of studies where the AFM provided pioneering information about the biology of complexes, and examples of studies where the simplicity of the method is used toward the development of potential diagnostic applications. (C) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码:351 / 367
页数:17
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