Protein-Protein and Protein-Ligand Interactions Studied by Electrospray- Ionization Mass Spectrometry

G.      Invernizzi; A.      Natalello; M.      Samalikova; R.      Grandori

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.

Keywords: Protein Complex Database, Penicillopepsin, Streptavidin, Lysozyme, protein-protein complexes, Electrospray-ionization mass spectrometry, non-covalent complexes, binding analysis, arginine repressor, lactoglobulin, tryptophan-repressor binding protein A

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Protein & Peptide Letters

Title:Protein-Protein and Protein-Ligand Interactions Studied by Electrospray- Ionization Mass Spectrometry

Volume: 14 Issue: 9

Author(s): G. Invernizzi, A. Natalello, M. Samalikova and R. Grandori

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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.

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Invernizzi G., Natalello A., Samalikova M. and Grandori R., Protein-Protein and Protein-Ligand Interactions Studied by Electrospray- Ionization Mass Spectrometry, Protein & Peptide Letters 2007; 14 (9) . https://dx.doi.org/10.2174/092986607782110301