Mass spectrometric analysis of protein interactions.
Mass spectrometry is a powerful tool for identification of interaction partners and structural characterization of protein interactions because of its high sensitivity, mass accuracy and tolerance towards sample heterogeneity. Several tools that allow studies of protein interaction are now available and recent developments that increase the confidence of studies of protein interaction by mass spectrometry include quantification of affinity-purified proteins by stable isotope labeling and reagents for surface topology studies that can be identified by mass-contributing reporters (e.g. isotope labels, cleavable cross-linkers or fragment ions. The use of mass spectrometers to study protein interactions using deuterium exchange and for analysis of intact protein complexes recently has progressed considerably.
Borch
Jonas
J
Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark.
Jørgensen
Thomas J D
TJ
Roepstorff
Peter
P
D000577:Amides / Q000737:chemistry; D002846:Chromatography, Affinity; D006859:Hydrogen / Q000737:chemistry; D013058:Mass Spectrometry / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D020349:Surface Plasmon Resonance
D000577:Amides; D011506:Proteins; D006859:Hydrogen