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.
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. © 2007 Bentham Science Publishers Ltd.
Invernizzi, G., Natalello, A., Samalikova, M., Grandori, R. (2007). Protein-protein and protein-ligand interactions studied by electrospray-ionization mass spectrometry. PROTEIN AND PEPTIDE LETTERS, 14(9), 894-902 [10.2174/092986607782110301].
Protein-protein and protein-ligand interactions studied by electrospray-ionization mass spectrometry
NATALELLO, ANTONINO;GRANDORI, RITA
2007
Abstract
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. © 2007 Bentham Science Publishers Ltd.
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