Protein-protein and protein-ligand interactions studied by electrospray-ionization mass spectrometry.
Preservation of non-covalent interactions in biopolymer mass spectrometry offers new approaches to binding analysis. Recent work from our laboratory is reviewed here and discussed with reference to recent literature in the field. Three issues are considered in particular: hydrophobically stabilized complexes, pH-dependent transitions, and linked protein-ligand and protein-protein binding equilibria.
Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milan, Italy. rita.grandori@unimib.it.
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Invernizzi
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Natalello
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Samalikova
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Grandori
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D019281:Dimerization; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D007782:Lactoglobulins / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism; D021241:Spectrometry, Mass, Electrospray Ionization
C087018:ArgR protein, Bacteria; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D007782:Lactoglobulins; D008024:Ligands; D011506:Proteins; D012097:Repressor Proteins; C081759:WrbA protein, E coli