Sickle cell hemoglobin with mutation at αHis-50 has improved solubility

Journal of Biological Chemistry

Volumn 290, Issue 35, 2015, Pages 21762-21772

  Tam, Ming F ^a   Tam, Tsuey Chyi S ^a   Simplaceanu, Virgil ^a   Ho, Nancy T ^a   Zou, Ming ^a   Ho, Chien ^a  

^a CARNEGIE MELLON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; DEXTRAN; ESCHERICHIA COLI; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PORPHYRINS;

ACIDIC CONDITIONS; AMINO ACID SUBSTITUTION; DOUBLE MUTANTS; ELEVATED TEMPERATURE; LATERAL CONTACT; SHORTER DELAYS; STRUCTURAL ALTERATIONS; SUBUNIT INTERFACES;

POLYMERS;

CARBOXYHEMOGLOBIN; DEOXYHEMOGLOBIN; GLUTAMINE; HEMOGLOBIN S; HISTIDINE; MUTANT PROTEIN; RECOMBINANT PROTEIN; TETRAMER; OXYGEN;

AMINO ACID SUBSTITUTION; ARTICLE; AUTOOXIDATION; BOHR EFFECT; CONTROLLED STUDY; ESCHERICHIA COLI; GENE MUTATION; HUMAN; OXYGEN AFFINITY; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; SOLUBILITY; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY; CHEMISTRY; GENETICS; KINETICS; METABOLISM; MUTATION; OXIDATION REDUCTION REACTION; TEMPERATURE;

HEMOGLOBIN, SICKLE; HISTIDINE; HUMANS; KINETICS; MUTATION; OXIDATION-REDUCTION; OXYGEN; POLYMERIZATION; PROTON MAGNETIC RESONANCE SPECTROSCOPY; RECOMBINANT PROTEINS; SOLUBILITY; TEMPERATURE;

EID: 84940688726     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.658054     Document Type: Article

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