The domains in γb-crystallin: identical fold-different stabilities
- 6 June 1997
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 269 (2) , 260-269
- https://doi.org/10.1006/jmbi.1997.1033
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Protein folding and association: In vitro studies for self-organization and targeting in the cellPublished by Elsevier ,1996
- High resolution structure of an oligomeric eye lens β-crystallinJournal of Molecular Biology, 1991
- X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteinsNature, 1990
- Calculation of protein extinction coefficients from amino acid sequence dataAnalytical Biochemistry, 1989
- cDNA Clones encoding bovine γ-crystallinsBiochemical and Biophysical Research Communications, 1987
- Folding and association of proteinsProgress in Biophysics and Molecular Biology, 1987
- Structural domains in proteins and their role in the dynamics of protein functionProgress in Biophysics and Molecular Biology, 1983
- Normal human lens—the distribution of proteinExperimental Eye Research, 1981
- The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin IINature, 1981
- Tertiary structure of Escherichia coli β-d-galactosidaseJournal of Molecular Biology, 1969