Protonation states of histidine and other key residues in deoxy normal human adult hemoglobin by neutron protein crystallography

The protonation states of the histidine residues key to the function of deoxy (T-state) human hemoglobin have been investigated using neutron protein crystallography. These residues can reversibly bind protons, thereby regulating the oxygen affinity of hemoglobin. By examining the OMIT F (o) − F (c)...

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Detalhes bibliográficos
Main Authors: Kovalevsky, Andrey, Chatake, Toshiyuki, Shibayama, Naoya, Park, Sam-Yong, Ishikawa, Takuya, Mustyakimov, Marat, Fisher, S. Zoe, Langan, Paul, Morimoto, Yukio
Formato: Artigo
Idioma:Inglês
Publicado em: International Union of Crystallography 2010
Assuntos:
Research Papers
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2967419/
https://ncbi.nlm.nih.gov/pubmed/21041929
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S0907444910025448
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