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    Mass spectrometry tools for analysis of intermolecular interactions

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    Authors
    Auclair, Jared R.
    Somasundaran, Mohan
    Green, Karin M.
    Evans, James E.
    Schiffer, Celia A.
    Ringe, Dagmar
    Petsko, Gregory A.
    Agar, Jeffrey N.
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Department of Pediatrics
    Document Type
    Book Chapter
    Publication Date
    2012-07-24
    Keywords
    Mass Spectrometry
    Protein Binding
    Binding Sites
    Biochemistry, Biophysics, and Structural Biology
    Molecular Biology
    Pharmacology, Toxicology and Environmental Health
    
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    Link to Full Text
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4638115/
    Abstract
    The small quantities of protein required for mass spectrometry (MS) make it a powerful tool to detect binding (protein-protein, protein-small molecule, etc.) of proteins that are difficult to express in large quantities, as is the case for many intrinsically disordered proteins. Chemical cross-linking, proteolysis, and MS analysis, combined, are a powerful tool for the identification of binding domains. Here, we present a traditional approach to determine protein-protein interaction binding sites using heavy water ((18)O) as a label. This technique is relatively inexpensive and can be performed on any mass spectrometer without specialized software.
    Source

    Methods Mol Biol. 2012;896:387-98. Link to article on publisher's site

    DOI
    10.1007/978-1-4614-3704-8_26
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/26024
    PubMed ID
    22821539
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    Link to Article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1007/978-1-4614-3704-8_26
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