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Ions of the interactome: The role of MS in the study of protein interactions in proteomics and structural biology
Author(s) -
Downard Kevin M.
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200600247
Subject(s) - interactome , proteomics , context (archaeology) , chemical biology , computational biology , tandem affinity purification , protein–protein interaction , chemistry , mass spectrometry , protein purification , biology , structural biology , quantitative proteomics , biochemistry , chromatography , affinity chromatography , paleontology , gene , enzyme
The role of MS in the study of protein‐protein interactions in solution is described from a proteomics perspective, in terms of high‐throughput analyses of protein complexes in vivo , through to chemical and biochemical treatments ahead of MS analysis in the context of complementary experimental approaches in structural biology. The use of MS to characterise protein‐protein interactions is described following the single and tandem affinity purification of protein complexes and assemblies of expressed proteins in host cells, the isolation and preservation of protein complexes on surfaces and microarrays, and their prior treatment with chemical and biochemical probes by hydrogen exchange, radical probe, chemical cross‐linking, and limited proteolysis. The advantages and disadvantages of each of the approaches are presented. These new and emerging applications, which further demonstrate the power of MS, continue to ensure that the mass spectrometer will remain at the heart of discoveries in proteomics in the foreseeable future.