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Determination of protein–protein interactions by matrix‐assisted laser desorption/ionization mass spectrometry
Author(s) -
Farmer Terry B.,
Caprioli Richard M.
Publication year - 1998
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/(sici)1096-9888(199808)33:8<697::aid-jms711>3.0.co;2-h
Subject(s) - chemistry , mass spectrometry , protein mass spectrometry , matrix assisted laser desorption/ionization , sample preparation in mass spectrometry , surface enhanced laser desorption/ionization , chromatography , desorption , matrix (chemical analysis) , ionization , analytical chemistry (journal) , tandem mass spectrometry , electrospray ionization , organic chemistry , ion , adsorption
A number of different procedures have been developed for use with matrix‐assisted laser desorption/ionization mass spectrometry (MALDI/MS) for the analysis of non‐covalent protein–protein complexes. These include use of specific matrix and laser combinations, accumulation of ‘first shot’ spectra, modification of pH and solvent conditions during sample preparation and use of cross‐linking agents to attach the monomers covalently to each other in the complex. The results have shown the techniques to be effective with some but not all complexes, although cross‐linking is the most successful. The physical and chemical nature of the complex is critical and therefore a diversity of approaches is recommended for such studies. © 1998 John Wiley & Sons, Ltd.