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 language | English |
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Pages | 123-124 |
Number of pages | 2 |
State | Published - 2002 |
Event | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: Jun 2 2002 → Jun 6 2002 |
Conference
Conference | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics |
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Country/Territory | United States |
City | Orlando, FL |
Period | 06/2/02 → 06/6/02 |