Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes
Version of Record online: 11 DEC 2003
Copyright © 2003 John Wiley & Sons, Ltd.
Journal of Mass Spectrometry
Volume 38, Issue 12, pages 1225–1237, December 2003
How to Cite
Sinz, A. (2003), Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes. J. Mass Spectrom., 38: 1225–1237. doi: 10.1002/jms.559
- Issue online: 11 DEC 2003
- Version of Record online: 11 DEC 2003
- chemical cross-linking;
- structural characterization;
- protein complexes
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.