Characterization of the ionizable groups interacting with anionic allosteric effectors of human hemoglobin.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference29 articles.
1. X-ray Diffraction Study of Binding of 2,3-Diphosphoglycerate to Human Deoxyhaemoglobin
2. Structure of inositol hexaphosphate–human deoxyhaemoglobin complex
3. Electrostatic interaction of hemoglobin and benzenepentacarboxylate
4. Allosteric effectors of hemoglobin. Interaction of human adult and fetal hemoglobins with poly(carboxylic acids)
5. Hemoglobin Deer Lodge (beta 2 His replaced by Arg). Consequences of altering the 2,3-diphosphoglycerate binding site.
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1. 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;2008-04-01
2. Liganded Hemoglobin Structural Perturbations by the Allosteric Effector L35;Biophysical Journal;2005-03
3. R-state hemoglobin bound to heterotropic effectors: models of the DPG, IHP and RSR13 binding sites;FEBS Letters;2004-12-24
4. Anaerobic Oxidations of Myoglobin and Hemoglobin by Spectroelectrochemistry;Methods in Enzymology;2002
5. Carbodiimide-Mediated Coupling of Benzenepentacarboxylate to Human Hemoglobin: Structural and Functional Consequences;Biomaterials, Artificial Cells and Immobilization Biotechnology;1992-01
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