Mass spectrometry-based approaches to protein-ligand interactions.
One of the greatest current challenges in proteomics is to develop an understanding of cellular communication and regulation processes, most of which involve noncovalent interactions of proteins with various binding partners. Mass spectrometry plays an important role in all aspects of these research efforts. This article provides a survey of mass spectrometry-based approaches for exploring protein-ligand interactions. A wide array of techniques is available, and the choice of method depends on the specific problem at hand. For example, the high-throughput screening of compound libraries for binding to a specific receptor requires different approaches than structural studies on multiprotein complexes. This review is directed to readers wishing to obtain a concise yet comprehensive overview of existing experimental techniques. Specific emphasis is placed on emerging methods that have been developed within the last few years.
Schermann
Sonya M
SM
Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. sonya.schermann@bioch.ox.ac.uk
Simmons
Douglas A
DA
Konermann
Lars
L
D000818:Animals; D003432:Cross-Linking Reagents / Q000737:chemistry; D041961:Deuterium Exchange Measurement; D006801:Humans; D008024:Ligands; D013058:Mass Spectrometry / Q000379:methods*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
D003432:Cross-Linking Reagents; D008024:Ligands; D011506:Proteins