Conformational and functional properties of haemoglobin in perturbed solvent: Relevance of electrostatic and hydrophobic interactions.
- 1 October 1989
- journal article
- research article
- Published by Elsevier in Journal of Molecular Liquids
- Vol. 42, 213-229
- https://doi.org/10.1016/0167-7322(89)80035-2
Abstract
No abstract availableThis publication has 45 references indexed in Scilit:
- Effect of some monohydric alcohols on the functional stability of bovine liver ?-galactosidaseBiopolymers, 1979
- Studies of the conformation of apomyoglobin in aqueous solutions and denaturing organic solventsBiopolymers, 1975
- Trypsin-organic solvent interaction. Simultaneous operation of competitive inhibition and dielectric effectBiochemistry, 1972
- Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of AllosteryNature, 1970
- Protein DenaturationAdvances in Protein Chemistry, 1968
- On the Conformational Stability of Globular ProteinsJournal of Biological Chemistry, 1965
- The Effect of Aprotic Dipolar Organic Solvents on the Kinetics of α-Chymotrypsin-Catalyzed Hydrolyses*Biochemistry, 1963
- The effect of aqueous alcohol solutions on the thermal transition of ribonucleaseBiochimica et Biophysica Acta, 1962
- Molecular kinetics of muscle adenosine triphosphatase. II. Solvent and structural effectsArchives of Biochemistry and Biophysics, 1953
- Solvent Effects in the α-Chymotrypsin—Hydrocinnamic Ester System1Journal of the American Chemical Society, 1952