Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry

Proceedings of the National Academy of Sciences of the United States of America
J J EnglanderVirgil L Woods

Abstract

An automated high-throughput, high-resolution deuterium exchange HPLC-MS method (DXMS) was used to extend previous hydrogen exchange studies on the position and energetic role of regulatory structure changes in hemoglobin. The results match earlier highly accurate but much more limited tritium exchange results, extend the analysis to the entire sequence of both hemoglobin subunits, and identify some energetically important changes. Allosterically sensitive amide hydrogens located at near amino acid resolution help to confirm the reality of local unfolding reactions and their use to evaluate resolved structure changes in terms of allosteric free energy.

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Citations

Sep 29, 2011·Journal of the American Society for Mass Spectrometry·Zhong-Yuan KanS Walter Englander
Jun 7, 2012·Journal of the American Society for Mass Spectrometry·Jiawei ChenMichael L Gross
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