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Volumn 39, Issue 45, 2000, Pages 13708-13718
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An additional H-bond in the α1β2 interface as the structural basis for the low oxygen affinity and high cooperativity of a novel recombinant hemoglobin (βL105W)
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Author keywords
[No Author keywords available]
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Indexed keywords
MUTANT PROTEIN;
RECOMBINANT HEMOGLOBIN;
ARTICLE;
CONTROLLED STUDY;
EXPRESSION VECTOR;
HYDROGEN BOND;
NONHUMAN;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
OXYGEN AFFINITY;
PRIORITY JOURNAL;
PROTEIN QUATERNARY STRUCTURE;
PROTEIN SYNTHESIS;
SITE DIRECTED MUTAGENESIS;
AMINO ACID SUBSTITUTION;
BINDING SITES;
CARBOXYHEMOGLOBIN;
HEMOGLOBIN A;
HEMOGLOBINS;
HUMANS;
HYDROGEN BONDING;
LEUCINE;
MUTAGENESIS, SITE-DIRECTED;
NITROGEN ISOTOPES;
NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;
OXYGEN;
PHYTIC ACID;
PROTEIN CONFORMATION;
PROTONS;
RECOMBINANT PROTEINS;
TEMPERATURE;
TRYPTOPHAN;
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EID: 0034649341
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi001115i Document Type: Article |
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Times cited : (18)
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References (41)
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