The conformational stability of α-crystallin is rather low: Calorimetric results
- 16 September 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 393 (2-3) , 151-154
- https://doi.org/10.1016/0014-5793(96)00867-8
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- On the thermal stability of .alpha.-crystallin: z new insight from infrared spectroscopyBiochemistry, 1995
- α-Crystallin-like Molecular Chaperone against the Thermal Denaturation of Lens Aldose Reductase: The Effect of Divalent Metal IonsBiochemical and Biophysical Research Communications, 1995
- Conformational stability of bovine holo and apo adrenodoxin — A scanning calorimetric studyProtein Science, 1995
- Structure and Modifications of the Junior Chaperone α‐CrystallinEuropean Journal of Biochemistry, 1994
- Apocytochrome P450cam is a native protein with some intermediate-like propertiesBiochemistry, 1993
- Junior chaperonesCurrent Biology, 1993
- Alpha-crystallin can function as a molecular chaperone.Proceedings of the National Academy of Sciences, 1992
- A differential scanning calorimetric study of the bovine lens crystallinsBiochemistry, 1989
- Heat‐induced changes in the conformation of α‐ and β‐crystalline: Unique thermal stability of α‐crystallinFEBS Letters, 1988
- A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric studyJournal of Molecular Biology, 1974