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Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes

Authors

  • Andrea Sinz

    Corresponding author
    1. Biotechnological–Biomedical Center, Faculty of Chemistry and Mineralogy, University of Leipzig, D-04103 Leipzig, Germany
    • Biotechnological–Biomedical Center, Faculty of Chemistry and Mineralogy, University of Leipzig, Linnéstrasse 3, D-04103 Leipzig, Germany.
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Abstract

Chemical cross-linking of proteins, an established method in protein chemistry, has gained renewed interest in combination with mass spectrometric analysis of the reaction products for elucidating low-resolution three-dimensional protein structures and interacting sequences in protein complexes. The identification of the large number of cross-linking sites from the complex mixtures generated by chemical cross-linking, however, remains a challenging task. This review describes the most popular cross-linking reagents for protein structure analysis and gives an overview of the strategies employing intra- or intermolecular chemical cross-linking and mass spectrometry. The various approaches described in the literature to facilitate detection of cross-linking products and also computer software for data analysis are reviewed. Cross-linking techniques combined with mass spectrometry and bioinformatic methods have the potential to provide the basis for an efficient structural characterization of proteins and protein complexes. Copyright © 2003 John Wiley & Sons, Ltd.

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