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J Am Soc Mass Spectrom. 2010 Apr;21(4):487-500. doi: 10.1016/j.jasms.2009.12.017. Epub 2010 Jan 4.

How far can we go with structural mass spectrometry of protein complexes?

Author information

  • Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel. michal.sharon@weizmann.ac.il

Abstract

Physical interactions between proteins and the formation of stable complexes form the basis of most biological functions. Therefore, a critical step toward understanding the integrated workings of the cell is to determine the structure of protein complexes, and reveal how their structural organization dictates function. Studying the three-dimensional organization of protein assemblies, however, represents a major challenge for structural biologists, due to the large size of the complexes, their heterogeneous composition, their flexibility, and their asymmetric structure. In the last decade, mass spectrometry has proven to be a valuable tool for analyzing such noncovalent complexes. Here, I illustrate the breadth of structural information that can be obtained from this approach, and the steps taken to elucidate the stoichiometry, topology, packing, dynamics, and shape of protein complexes. In addition, I illustrate the challenges that lie ahead, and the future directions toward which the field might be heading.

2010 American Society for Mass Spectrometry. Published by Elsevier Inc. All rights reserved.

PMID:
20116283
[PubMed - indexed for MEDLINE]
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