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Volumn 402, Issue 1, 2002, Pages 59-64
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The carbon monoxide derivative of human hemoglobin carrying the double mutation LeuB10 → Tyr and HisE7 → Gln on α and β chains probed by infrared spectroscopy
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Author keywords
Hemoglobin mutants; Human hemoglobin; Infrared spectroscopy; Ligand binding in hemoproteins
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Indexed keywords
CARBON MONOXIDE;
GLUTAMINE;
HEMOGLOBIN;
HEMOGLOBIN A;
HEMOGLOBIN BETA CHAIN;
HISTIDINE;
IRON;
LEUCINE;
MUTANT PROTEIN;
TYROSINE;
ARTICLE;
GENE MUTATION;
HUMAN;
HYDROGEN BOND;
INFRARED SPECTROSCOPY;
KINETICS;
MOLECULAR INTERACTION;
MUTANT;
PRIORITY JOURNAL;
PROTEIN LOCALIZATION;
PROTEIN STABILITY;
TECHNIQUE;
AMINO ACID SUBSTITUTION;
CARBON MONOXIDE;
CARBOXYHEMOGLOBIN;
GLUTAMINE;
HEME;
HEMOGLOBIN A;
HISTIDINE;
HUMANS;
HYDROGEN BONDING;
IRON;
KINETICS;
LEUCINE;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, SECONDARY;
SPECTROSCOPY, FOURIER TRANSFORM INFRARED;
STRUCTURE-ACTIVITY RELATIONSHIP;
TYROSINE;
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EID: 0036612751
PISSN: 00039861
EISSN: None
Source Type: Journal
DOI: 10.1016/S0003-9861(02)00061-9 Document Type: Article |
Times cited : (2)
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References (15)
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