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

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.

SUBMITTER: Englander JJ 

PROVIDER: S-EPMC165829 | biostudies-literature | 2003 Jun

REPOSITORIES: biostudies-literature

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

Englander Joan J JJ   Del Mar Charyl C   Li Will W   Englander S Walter SW   Kim Jack S JS   Stranz David D DD   Hamuro Yoshitomo Y   Woods Virgil L VL  

Proceedings of the National Academy of Sciences of the United States of America 20030528 12

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 a  ...[more]

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