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Effector-Induced Structural Fluctuation Regulates the Ligand Affinity of an Allosteric Protein: Binding of Inositol Hexaphosphate Has Distinct Dynamic Consequences for the T and R States of Hemoglobin

The present study reports distinct dynamic consequences for the T- and R-states of human normal adult hemoglobin (Hb A) due to the binding of a heterotropic allosteric effector, inositol hexaphosphate (IHP). A nuclear magnetic resonance (NMR) technique based on modified transverse relaxation optimiz...

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Библиографические подробности
Главные авторы: Song, Xiang-jin, Simplaceanu, Virgil, Ho, Nancy T., Ho, Chien
Формат: Artigo
Язык:Inglês
Опубликовано: 2008
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Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC2493540/
https://ncbi.nlm.nih.gov/pubmed/18376851
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi7023699
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