Liganded hemoglobin structural perturbations by the allosteric effector L35

Biophysical Journal

Volumn 88, Issue 3, 2005, Pages 2057-2067

  Chen, Qiuying ^a   Lalezari, Iraj ^b   Nagel, Ronald L ^a,c   Hirsch, Rhoda Elison ^a,d  

^a Division of Hematology   (United States)

^b MONTEFIORE MEDICAL CENTER   (United States)

^c Department of Physiology and Biophysics ^*  (United States)

^d ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BEZAFIBRATE; EFFECTOR L35; HEME; PHYTIC ACID; UNCLASSIFIED DRUG; CARBANILAMIDE DERIVATIVE; HEMOGLOBIN; L 35; LIGAND;

ALLOSTERISM; ARTICLE; BINDING KINETICS; BINDING SITE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CORRELATION ANALYSIS; FLUORESCENCE; HEMOGLOBIN ANALYSIS; MASS SPECTROMETRY; OXYGEN AFFINITY; PH; PROTEIN CONFORMATION; STEADY STATE; STRUCTURE ANALYSIS; SURFACE PLASMON RESONANCE; CHEMISTRY; PROTEIN BINDING; SPECTROFLUOROMETRY; STEREOISOMERISM; STRUCTURE ACTIVITY RELATION;

BINDING SITES; HEMOGLOBINS; LIGANDS; PHENYLUREA COMPOUNDS; PROTEIN BINDING; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; STEREOISOMERISM; STRUCTURE-ACTIVITY RELATIONSHIP; SURFACE PLASMON RESONANCE;

EID: 21244479077     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.046136     Document Type: Article

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