Current limitations in native mass spectrometry based structural biology - PubMed (original) (raw)

Current limitations in native mass spectrometry based structural biology

Esther van Duijn. J Am Soc Mass Spectrom. 2010 Jun.

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Abstract

Nowadays, mass spectrometry plays an important role in structural biology. At one end it can be used to investigate intact protein complexes, providing details about the complex composition, topology, stability, and dynamics, whereas at the other end the protein's identity and possible modifications can be visualized using proteomics approaches. Combining all this information allows the generation of detailed models for functional biological assemblies. Here, a perspective on the application of native mass spectrometry in structural biology is presented. The potential of this technique and some important current limitations are discussed. This includes issues regarding the quality/homogeneity of the sample, the dissociation efficiency of protein complexes during tandem mass spectrometric analysis, and some boundaries of ion mobility mass spectrometry.

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

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References

    1. J Biol Chem. 2008 Oct 17;283(42):28513-7 - PubMed
    1. Proc Natl Acad Sci U S A. 2008 Nov 25;105(47):18139-44 - PubMed
    1. Curr Opin Chem Biol. 2004 Oct;8(5):519-26 - PubMed
    1. Chemistry. 2005 Jan 21;11(3):960-8 - PubMed
    1. Curr Protoc Protein Sci. 2010 Nov;Chapter 17:Unit17.12 - PubMed

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