The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 1. Microstate linear free energy relations

Biochemistry

Volumn 43, Issue 38, 2004, Pages 12048-12064

  Goldbeck, Robert A ^a   Esquerra, Raymond M ^b   Holt, Jo M ^c   Ackers, Gary K ^c   Kliger, David S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b SAN FRANCISCO STATE UNIVERSITY   (United States)

^c WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENERGY; DATA REDUCTION; FREE ENERGY; PARAMETER ESTIMATION; REACTION KINETICS; THERMODYNAMICS;

HEMOGLOBIN ALLOSTERY; LIGAND BINDING; LIGATION MICROSTATES; LINEAR FREE ENERGY; REACTION ENERGY PERTURBATION;

HEMOGLOBIN;

HEMOGLOBIN;

ALLOSTERISM; ARTICLE; CALCULATION; CHEMICAL REACTION KINETICS; LIGAND BINDING; MOLECULAR DYNAMICS; PHASE TRANSITION; PHOTOLYSIS; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; REACTION ANALYSIS; STATISTICAL MODEL; STRAIN DIFFERENCE; THERMODYNAMICS;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; CARBON MONOXIDE; HEMOGLOBINS; KINETICS; LIGANDS; PHOTOLYSIS; PHYTIC ACID; PROTEIN STRUCTURE, QUATERNARY; SPECTRUM ANALYSIS; THERMODYNAMICS;

EID: 4644320185     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049393v     Document Type: Article

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