Chemical cross-linking in the structural analysis of protein assemblies
| Autor: | Hieu T. Nguyen, Daniel T. Thornton, Feixia Chu |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Protein interface Models Molecular Computer science Protein Conformation Sample processing Proteins Computational biology Mass spectrometric General Biochemistry Genetics and Molecular Biology Mass Spectrometry Article Medium resolution 03 medical and health sciences 030104 developmental biology Cross-Linking Reagents Protein Interaction Mapping Primary sequence Molecular Biology Protein Binding |
| Zdroj: | Methods (San Diego, Calif.). 144 |
| ISSN: | 1095-9130 |
| Popis: | For decades, chemical cross-linking of proteins has been an established method to study protein interaction partners. The chemical cross-linking approach has recently been revived by mass spectrometric analysis of the cross-linking reaction products. Chemical cross-linking and mass spectrometric analysis (CXMS) enables the identification of residues that are close in three-dimensional (3D) space but not necessarily close in primary sequence. Therefore, this approach provides medium resolution information to guide de novo structure prediction, protein interface mapping and protein complex model building. The robustness and compatibility of the CXMS approach with multiple biochemical methods have made it especially appealing for challenging systems with multiple biochemical compositions and conformation states. This review provides an overview of the CXMS approach, describing general procedures in sample processing, data acquisition and analysis. Selection of proper chemical cross-linking reagents, strategies for cross-linked peptide identification, and successful application of CXMS in structural characterization of proteins and protein complexes are discussed. |
| Databáze: | OpenAIRE |
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