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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Autores principales: Kovalevsky, Andrey, Chatake, Toshiyuki, Shibayama, Naoya, Park, Sam-Yong, Ishikawa, Takuya, Mustyakimov, Marat, Fisher, S. Zoe, Langan, Paul, Morimoto, Yukio
Formato: Artigo
Lenguaje:Inglês
Publicado: International Union of Crystallography 2010
Materias:
Research Papers
Acceso en línea: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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