Protein-protein interactions: nature of the electrostatic stabilization of deoxyhemoglobin tetramer formation

The summed electrostatic free energy contributions to deoxyhemoglobin A0 tetramer formation were computed at a series of pH and ionic strength values as the difference between the computed values for the tetramer and for the sum of the four individual chains. The electrostatic stabilization of each...

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Veröffentlicht in:	Biochemistry (Easton) 1981-02, Vol.20 (3), p.580-586
Hauptverfasser:	Friend, Stephen H, Matthew, James B, Gurd, Frank R. N
Format:	Artikel
Sprache:	eng
Schlagworte:	Calorimetry Drug Stability Hemoglobins Humans Hydrogen-Ion Concentration Kinetics Macromolecular Substances Protein Conformation Thermodynamics
Online-Zugang:	Volltext
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