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Expert Rev Proteomics. 2006 Aug;3(4):399-408.

Photoaffinity labeling combined with mass spectrometric approaches as a tool for structural proteomics.

Author information

1
University of North Carolina at Chapel Hill, UNC-Duke Proteomics Core Facility, Department of Biochemistry and Biophysics, CB7028, Chapel Hill, NC 27599, USA. robinett@med.unc.edu

Abstract

Protein chemistry, such as crosslinking and photoaffinity labeling, in combination with modern mass spectrometric techniques, can provide information regarding protein-protein interactions beyond that normally obtained from protein identification and characterization studies. While protein crosslinking can make tertiary and quaternary protein structure information available, photoaffinity labeling can be used to obtain structural data about ligand-protein interaction sites, such as oligonucleotide-protein, drug-protein and protein-protein interaction. In this article, we describe mass spectrometry-based photoaffinity labeling methodologies currently used and discuss their current limitations. We also discuss their potential as a common approach to structural proteomics for providing 3D information regarding the binding region, which ultimately will be used for molecular modeling and structure-based drug design.

PMID:
16901199
PMCID:
PMC2266983
DOI:
10.1586/14789450.3.4.399
[Indexed for MEDLINE]
Free PMC Article

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