Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and 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.
Sinz
Andrea
A
Biotechnological-Biomedical Center, Faculty of Chemistry and Mineralogy, University of Leipzig, D-04103 Leipzig, Germany. sinz@chemie.uni-leipzig.de
D001665:Binding Sites; D003432:Cross-Linking Reagents / Q000737:chemistry*; D007553:Isotope Labeling; D046911:Macromolecular Substances; D013058:Mass Spectrometry / Q000379:methods*; D015394:Molecular Structure; D010449:Peptide Mapping; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012984:Software
D003432:Cross-Linking Reagents; D046911:Macromolecular Substances; D011506:Proteins