Proton-Deuteron Amide Exchange Studies by MS and NMR: a New Method for Protein NMR Resonance Assignment

摘要

Here we explore a novel approach for protein resonance assignment that relies on the ability of Mass Spectrometry (MS) and nuclear magnetic resonance (NMR) to monitor the rates of exchange of an amide proton for a water deuteron. MS can provide information on the peptide sequence containing a position that exchanges, while NMR can provide resolved cross peaks that yield structure and drug binding information. By correlating amide exchange rates from the two sources, we hope to achieve the assignment of NMR peaks from proteins that are difficult to pursue by the usual triple resonance NMR techniques.