期刊
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
卷 24, 期 3, 页码 444-449出版社
SPRINGER
DOI: 10.1007/s13361-012-0565-x
关键词
Cross-linking; Proteins; Cross-linked peptides; Ionmobility spectrometry; Mass Spectrometry; Liquid chromatography; Drift time; Protein structure; Heavy isotope labeling
资金
- National Institute of General Medical Sciences (NIGMS) [GM094623]
- National Institute of Allergy and Infectious Diseases [IAA Y1-AI-8401-01]
- NIGMS [8 P41 GM103493-10]
- US Department of Energy/Office of Biological and Environmental Research (DOE/BER)
Chemical cross-linking of proteins followed by proteolysis and mass spectrometric analysis of the resulting cross-linked peptides provides powerful insight into the quaternary structure of protein complexes. Mixed-isotope cross-linking (a method for distinguishing intermolecular cross-links) was coupled with liquid chromatography, ion mobility spectrometry and mass spectrometry (LC-IMS-MS) to provide an additional separation dimension to the traditional cross-linking approach. This method produced multiplet m/z peaks that are aligned in the IMS drift time dimension and serve as signatures of intermolecular cross-linked peptides. We developed an informatics tool to use the amino acid sequence information inherent in the multiplet spacing for accurate identification of the cross-linked peptides. Because of the separation of cross-linked and non-cross-linked peptides in drift time, our LC-IMS-MS approach was able to confidently detect more intermolecular cross-linked peptides than LC-MS alone.
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