Effector-induced structural fluctuation regulates the ligand affinity of an allosteric protein: Binding of inositol hexaphosphate has distinct dynamic consequences for the T and R states of hemoglobin

Biochemistry

Volumn 47, Issue 17, 2008, Pages 4907-4915

  Song, Xiang Jin ^a   Simplaceanu, Virgil ^a   Ho, Nancy T ^a   Ho, Chien ^a  

^a CARNEGIE MELLON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CHEMICAL SHIFT; CONFORMATIONS; CRYSTALLOGRAPHY; EXCHANGE INTERACTIONS; LIGANDS; MOLECULAR DYNAMICS; PHOSPHATES;

ALLOSTERIC PROTEINS; CHEMICAL SHIFT ANISOTROPY (CSA); CONFORMATIONAL EXCHANGE; INOSITOL HEXAPHOSPHATE; LIGAND AFFINITY; STRUCTURAL FLUCTUATION;

PROTEINS;

AMINO ACID; DEOXYHEMOGLOBIN; DIMER; HEMOGLOBIN; HEMOGLOBIN A; HISTIDINE; LIGAND; LYSINE; PHYTIC ACID; POLYPEPTIDE; VALINE; CARBOXYHEMOGLOBIN; HEME;

ALLOSTERISM; ANISOTROPY; ARTICLE; BETA SHEET; BINDING AFFINITY; BINDING SITE; CONFORMATIONAL TRANSITION; CRYSTALLOGRAPHY; NUCLEAR MAGNETIC RESONANCE; OXYGENATION; PRIORITY JOURNAL; PROTEIN STRUCTURE; SPECTROSCOPY; TRANSVERSE RELAXATION OPTIMIZED SPECTROSCOPY; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; DRUG EFFECT; HUMAN; METABOLISM; MOVEMENT (PHYSIOLOGY); NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING; PROTEIN QUATERNARY STRUCTURE; TIME;

ALLOSTERIC REGULATION; CARBOXYHEMOGLOBIN; DIMERIZATION; HEME; HEMOGLOBIN A; HUMANS; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOVEMENT; PHYTIC ACID; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; TIME FACTORS;

EID: 42449097652     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7023699     Document Type: Article

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