Article
NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
International journal of biological macromolecules - 1 Jan 2000
Carver J A, Lindner R A
Abstract excerpt
The subunit molecular mass of alpha-crystallin, like many small heat-shock proteins (sHsps), is around 20 kDa although the protein exists as a large aggregate of average mass around 800 kDa. Despite this large size, a well-resolved 1H NMR spectrum is observed for alpha-crystallin which arises fro...
Topics
- Aging
- Amino Acid Sequence
- Animals
- Crystallins
- Heat-Shock Proteins
- In Vitro Techniques
- Macromolecular Substances
- Magnetic Resonance Spectroscopy
- Mice
- Models, Molecular
- Molecular Chaperones
- Molecular Sequence Data
- Molecular Weight
- Mutation
- Neoplasm Proteins
- Protein Conformation
- Protein Denaturation
- Urea