A general mass spectrometry-based method for the quantitation of protein-ligand binding interactions in solution


Journal Article

The protein-ligand binding interactions in solution were investigated using mass spectrometry. The H/D exchange and mass spectrometry-based technique termed as stability of unpurified proteins by rates of H/D exchange (SUPREX) was developed to evaluate thermodynamic stability of proteins. The analysis was initiated by 10-fold dilution of stock solution of protein in series of deuterated exchange buffers which varied in concentration of deuterated guanidine. The results show that increased H/D time shifted the SUPREX curve transition midpoint to lower denaturant.

Duke Authors

Cited Authors

  • Fitzgerald, MC; Powell, KD; Wang, MZ; Ma, L; Ghaemmaghami, S; Oas, TG

Published Date

  • December 1, 2002

Published In

  • Proceedings 50th Asms Conference on Mass Spectrometry and Allied Topics

Start / End Page

  • 395 - 396

Citation Source

  • Scopus