@article {Invernizzi:2007:0929-8665:894,
title = "Protein-Protein and Protein-Ligand Interactions Studied by Electrospray- Ionization Mass Spectrometry",
journal = "Protein and Peptide Letters",
parent_itemid = "infobike://ben/ppl",
publishercode ="ben",
year = "2007",
volume = "14",
number = "9",
publication date ="2007-09-01T00:00:00",
pages = "894-902",
itemtype = "ARTICLE",
issn = "0929-8665",
url = "https://www.ingentaconnect.com/content/ben/ppl/2007/00000014/00000009/art00011",
doi = "doi:10.2174/092986607782110301",
keyword = "arginine repressor, tryptophan-repressor binding protein A, Electrospray-ionization mass spectrometry, binding analysis, lactoglobulin, non-covalent complexes",
author = "Invernizzi, G. and Natalello, A. and Samalikova, M. and Grandori, R.",
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. ",
}