Article
The mutation Asp69-->Ser affects the chaperone-like activity of alpha A-crystallin.
European journal of biochemistry - 15 Sept 1995
Smulders R H, Merck K B, Aendekerk J, Horwitz J, Takemoto L, Slingsby C, Bloemendal H, De Jong W W
Abstract excerpt
alpha-Crystallins are members of the family of small heat-shock proteins. The conformation and mode of action of these 'junior chaperones' are unknown. To investigate the structure and chaperone-like activity, four mutants of bovine alpha A-crystallin were generated by site-directed mutagenesis....
Topics
- Amino Acid Sequence
- Asparagine
- Base Sequence
- Chromatography, Gel
- Crystallins
- DNA Mutational Analysis
- Escherichia coli
- Fluorescence
- Hot Temperature
- Molecular Chaperones
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation
- Protein Folding
- Serine
- Structure-Activity Relationship
- Surface Properties