| Literature DB >> 12773622 |
Joan J Englander1, Charyl Del Mar, Will Li, S Walter Englander, Jack S Kim, David D Stranz, Yoshitomo Hamuro, Virgil 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.Entities:
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Year: 2003 PMID： 12773622 PMCID： PMC165829 DOI： 10.1073/pnas.1232301100
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205