Mutations of the βN102 residue of HbA not only inhibit the ligand-linked T to Re state transition, but also profoundly affect the properties of the T state itself

Biochemistry

Volumn 46, Issue 7, 2007, Pages 2037-2049

  Kwiatkowski, Laura D ^a   Hui, Hilda L ^a   Karasik, Ellen ^a   Colby, Judith E ^a   Noble, Robert W ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN BONDS; MUTAGENESIS; OXYGEN; PH EFFECTS; PHOSPHATES; SUBSTITUTION REACTIONS;

BOHR EFFECTS; QUATERNARY STATE; STATE TRANSITION; TETRAMERS;

HEMOGLOBIN;

ASPARAGINE; ASPARTIC ACID; HEMOGLOBIN A; OXYGEN; PHYTIC ACID; CARBON MONOXIDE; GLYCINE; LIGAND; PROTEIN SUBUNIT;

ALPHA CHAIN; AMINO ACID SUBSTITUTION; ARTICLE; BETA CHAIN; BINDING AFFINITY; CHEMICAL REACTION KINETICS; CONFORMATIONAL TRANSITION; HUMAN; HYDROGEN BOND; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; CHEMISTRY; GENETICS; KINETICS; LIGHT; MUTATION; PHOTOCHEMISTRY; PROTEIN BINDING;

AMINO ACID SUBSTITUTION; ASPARTIC ACID; CARBON MONOXIDE; GLYCINE; HEMOGLOBIN A; HUMANS; KINETICS; LIGANDS; LIGHT; MUTATION; OXYGEN; PHOTOCHEMISTRY; PHYTIC ACID; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS;

EID: 33847048655     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061668e     Document Type: Article

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