H/D exchange and equilibrium titration for understanding protein-ligand interactions: Calmodulin/metal ion/peptide and FABP/fatty acid interactions

Mei Zhu, Don L. Rempel, Daryl E. Giblin, Michael L. Gross, Benhur Ogbay, David Cistola

Research output: Contribution to conferencePaperpeer-review

Abstract

H/D exchange and electrospary ionization (ESI) mass spectrometry (MS) were used to probe protein-ligand interactions. The proten-ligand binding and the induced conformational changes were used to control the activity of regulatory proteins and to interconvert mechanical work and physicochemical free energy. The immobilized protein was back-exchanged and desalted with ice-cold formic-acid solution and the resulting protein was eluted by using an isocratic flow of solvent with high organic composition. The results show a 1:4 CaM:Ca complex in CAM by titrating apo-CAM with Ca 2+, a 1:1 CaM:peptide complex in holo-CaM by titrating with melittin (ML) or mastoparan (MP).

Original languageEnglish
Pages123-124
Number of pages2
StatePublished - 2002
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002Jun 6 2002

Conference

ConferenceProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Country/TerritoryUnited States
CityOrlando, FL
Period06/2/0206/6/02

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