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

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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.





Keywords: Electrospray-ionization mass spectrometry; arginine repressor; binding analysis; lactoglobulin; non-covalent complexes; tryptophan-repressor binding protein A

Document Type: Research Article

DOI: https://doi.org/10.2174/092986607782110301

Publication date: 2007-09-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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