Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride (IV) Dependence of the N ⇌ A transconformation on temperature
- 1 January 1977
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 490 (1) , 200-208
- https://doi.org/10.1016/0005-2795(77)90120-9
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Three-state denaturation of α-lactalbumin by guanidine hydrochlorideJournal of Molecular Biology, 1976
- Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride (II)Biochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochlorideBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973
- Kinetics of unfolding and refolding of proteinsJournal of Molecular Biology, 1973
- Inter- and intramolecular interactions of α-lactalbumin: XII. Changes in the environment of aromatic residues in the goat proteinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1972
- Potentiometric titration studies on globular proteinsBiopolymers, 1972
- Thermodynamics of the denaturation of ribonuclease by guanidine hydrochlorideBiochemistry, 1970
- Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. III. Dependence on temperatureBiochemistry, 1970
- Equilibrium and kinetics of the unfolding of lysozyme (muramidase) by guanidine hydrochlorideJournal of Molecular Biology, 1966
- Inter- and Intramolecular Interactions of α-Lactalbumin. II. Aggregation Reactions at Acid pH*Biochemistry, 1964