Chemical cross-linking and native mass spectrometry: A fruitful combination for structural biology |
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Authors: | Andrea Sinz Christian Arlt Dror Chorev Michal Sharon |
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Affiliation: | 1.Department of Pharmaceutical Chemistry & Bioanalytics, Institute of Pharmacy, Martin-Luther University Halle-Wittenberg, D-06120, Halle, Germany;2.Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, 76100, Israel |
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Abstract: | Mass spectrometry (MS) is becoming increasingly popular in the field of structural biology for analyzing protein three-dimensional-structures and for mapping protein–protein interactions. In this review, the specific contributions of chemical crosslinking and native MS are outlined to reveal the structural features of proteins and protein assemblies. Both strategies are illustrated based on the examples of the tetrameric tumor suppressor protein p53 and multisubunit vinculin-Arp2/3 hybrid complexes. We describe the distinct advantages and limitations of each technique and highlight synergistic effects when both techniques are combined. Integrating both methods is especially useful for characterizing large protein assemblies and for capturing transient interactions. We also point out the future directions we foresee for a combination of in vivo crosslinking and native MS for structural investigation of intact protein assemblies. |
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Keywords: | chemical cross-linking native mass spectrometry protein 3D structure protein-protein interactions |
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