The Thermodynamics of myoglobin stability effects of axial ligand
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference26 articles.
1. Reversible Denaturation of Sperm Whale Myoglobin. I. Dependence on Temperature, pH, and Composition
2. The Stabilization of Horse Ferrihemoglobin to Acid Denaturation by Combination with Ligands*
3. Axial ligand effects on myoglobin stability.
4. Electrostatic stabilization in myoglobin. The pH dependence of summed electrostatic contributions
5. Thermal stability of hemoglobin and myoglobin
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1. Possible Mechanism for Cold Denaturation of Proteins at High Pressure;Physical Review Letters;2003-09-26
2. The temperature dependence of the kinetics of cyanide dissociation from the cyanide complex of myoglobin studied by cyclic voltammetry;Journal of Electroanalytical Chemistry;1999-05
3. Role of non-compatible osmolytes in the stabilization of proteins during heat stress;Biochemical Journal;1998-01-01
4. Temperature dependence of histidine ionization constants in myoglobin;Biophysical Journal;1997-12
5. Heat and Cold Denatured States of Monomeric λ Repressor Are Thermodynamically and Conformationally Equivalent;Biochemistry;1996-01-01
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