Direct determination of protonation states of histidine residues in a 2 Å neutron structure of deoxy-human normal adult hemoglobin and implications for the bohr effect

Journal of Molecular Biology

Volumn 398, Issue 2, 2010, Pages 276-291

  Kovalevsky, Andrey Y ^a   Chatake, Toshiyuki ^b   Shibayama, Naoya ^c   Park, Sam Yong ^d   Ishikawa, Takuya ^b   Mustyakimov, Marat ^a   Fisher, Zoe ^a   Langan, Paul ^a   Morimoto, Yukio ^b  

^a LOS ALAMOS NATIONAL LABORATORY   (United States)

^b KYOTO UNIVERSITY   (Japan)

^c JICHI MEDICAL UNIVERSITY   (Japan)

^d YOKOHAMA CITY UNIVERSITY   (Japan)

Author keywords

Bohr effect; Hemoglobin; Histidine; Neutron protein crystallography; Protonation state

Indexed keywords

DEOXYHEMOGLOBIN; HISTIDINE;

ARTICLE; BOHR EFFECT; CONTROLLED STUDY; CRYSTALLOGRAPHY; DEUTERIUM HYDROGEN EXCHANGE; HUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON TRANSPORT;

EID: 77951768618     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.03.016     Document Type: Article

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