Journal
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
Volume 21, Issue 4, Pages 487-500Publisher
AMER CHEMICAL SOC
DOI: 10.1016/j.jasms.2009.12.017
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Funding
- Morasha Program
- Israel Science Foundation [1823/07]
- Josef Cohn Minerva Center for Biomembrane Research
- Chais Family Fellows Program for New Scientists
- Abraham and Sonia Rochlin Foundation
- Wolfson Family Charitable Trust
- Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly
- estate of Shlomo and Sabine Beirzwinsky
- Meil de Botton Aynsley and Karen Siem, UK
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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. (J Am Soc Mass Spectrom 2010, 21, 487-500) (C) 2010 American Society for Mass Spectrometry
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