Chemical Cross-linking Mass Spectrometry for Profiling Protein Structures and Protein-Protein Interactions
نویسندگان
چکیده
منابع مشابه
Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions.
Closely related to studying the function of a protein is the analysis of its three-dimensional structure and the identification of interaction sites with its binding partners. An alternative approach to the high-resolution methods for three-dimensional protein structure analysis, such as X-ray crystallography and NMR spectroscopy, consists of covalently connecting two functional groups of the p...
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Mitochondrial protein interactions and complexes facilitate mitochondrial function. These complexes range from simple dimers to the respirasome supercomplex consisting of oxidative phosphorylation complexes I, III, and IV. To improve understanding of mitochondrial function, we used chemical cross-linking mass spectrometry to identify 2,427 cross-linked peptide pairs from 327 mitochondrial prote...
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Chemical cross-linking of reactive groups in native proteins and protein complexes in combination with the identification of cross-linked sites by mass spectrometry has been in use for more than a decade. Recent advances in instrumentation, cross-linking protocols, and analysis software have led to a renewed interest in this technique, which promises to provide important information about nativ...
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GRAPHICAL ABSTRACT ABSTRACT Chemical cross-linking coupled with mass spectrometry (CXMS) identifies protein residues that are close in space, and has been increasingly used for modeling the structures of protein complexes. Here we show that a single structure is usually sufficient to account for the intermolecular cross-links identified for a stable complex with sub-µmol/L binding affinity. ...
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ژورنال
عنوان ژورنال: Journal of Proteomics & Bioinformatics
سال: 2015
ISSN: 0974-276X
DOI: 10.4172/jpb.10000e28