Determination of Oxygen Binding Properties of the Individual Subunits of Intact Human Adult Hemoglobin
Author:
Publisher
The Chemical Society of Japan
Subject
General Chemistry
Reference27 articles.
1. THE STEREOCHEMICAL MECHANISM OF THE COOPERATIVE EFFECTS IN HEMOGLOBIN REVISITED
2. The Molecular Code for Hemoglobin Allostery Revealed by Linking the Thermodynamics and Kinetics of Quaternary Structural Change. 1. Microstate Linear Free Energy Relations
3. The Molecular Code for Hemoglobin Allostery Revealed by Linking the Thermodynamics and Kinetics of Quaternary Structural Change. 2. Cooperative Free Energies of (αFeCOβFe)2 and (αFeβFeCO)2 T-State Tetramers
4. A Comparative NMR Study of the Polypeptide Backbone Dynamics of Hemoglobin in the Deoxy and Carbonmonoxy Forms
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1. Structural origin of cooperativity in human hemoglobin: a view from different roles of α and β subunits in the α2β2 tetramer;Biophysical Reviews;2022-04
2. Heterogeneity between Two α Subunits of α2β2 Human Hemoglobin and O2 Binding Properties: Raman, 1H Nuclear Magnetic Resonance, and Terahertz Spectra;Biochemistry;2017-11-07
3. An Origin of Cooperative Oxygen Binding of Human Adult Hemoglobin: Different Roles of the α and β Subunits in the α2β2 Tetramer;PLOS ONE;2015-08-05
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