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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