Title

Mass spectrometry tools for analysis of intermolecular interactions

UMMS Affiliation

Department of Pediatrics; Department of Biochemistry and Molecular Pharmacology

Publication Date

2012-07-24

Document Type

Book Chapter

Subjects

Mass Spectrometry; Protein Binding; Binding Sites

Disciplines

Biochemistry, Biophysics, and Structural Biology | Molecular Biology | Pharmacology, Toxicology and Environmental Health

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.

DOI of Published Version

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

Source

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

Journal/Book/Conference Title

Methods in molecular biology (Clifton, N.J.)

Related Resources

Link to Article in PubMed

PubMed ID

22821539

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