Equilibrium Aspects of the Binding of myo-Inositol Hexakisphosphate to Human Hemoglobin as Studied by 31P NMR and pH-Stat Techniques
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1981.tb05489.x/fullpdf
Reference30 articles.
1. The structure of myo-inositol hexaphosphate dodecasodium salt octatriacontahydrate: A single crystal X-ray analysis
2. Conformational states of myo-inositol hexakis(phosphate) in aqueous solution. A carbon-13 NMR, phosphorus-31 NMR, and Raman spectroscopic investigation
3. A NEW TYPE OF PHOSPHORIC ACID COMPOUND ISOLATED FROM BLOOD, WITH SOME REMARKS ON THE EFFECT OF SUBSTITUTION ON THE ROTATION OF l-GLYCERIC ACID
4. Structure of "phytic acids"
5. The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin
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2. Solution Structure and Dynamics of Human Hemoglobin in the Carbonmonoxy Form;Biochemistry;2013-08-15
3. Non-Canonical Ligand-Binding Events as Detected by NMR;Recent Developments in Biomolecular NMR;2012-08-01
4. Transition of haemoglobin between two tertiary conformations: Inositol hexakisphosphate increases the transition constant and the affinity of sheep haemoglobin for 5,5′-dithiobis(2-nitrobenzoate);Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2009-03
5. 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
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