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

Critical Insight

DOI: 10.1016/j.jasms.2009.12.017

Cite this article as:
Sharon, M. J Am Soc Mass Spectrom (2010) 21: 487. doi:10.1016/j.jasms.2009.12.017


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.

Copyright information

© American Society for Mass Spectrometry 2010

Authors and Affiliations

  1. 1.Department of Biological ChemistryWeizmann Institute of ScienceRehovotIsrael

Personalised recommendations