Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
More | small heat shock protein, alphaA-crystallin, functions as a molecular chaperone, and enhances thermal stability of both delta-crystallin and ASL. Thermal unfolding of delta-crystallin or ASL in the presence of alphaA-crystallin follows a similar three-state model. A stable intermediate which retains about 30% alpha-helical structure is observed. Protection from thermal denaturation by alphaA-crystallin is by interaction with partly unfolded ASL to form high molecular weight heteroligomers. Aggregate formation of ASL is significantly reduced in the presence of alphaA-crystallin. The extent of protection of ASL at different ratios of alpahA-crystallin is described by hyperbolic curves, suggesting the preferential recognition of partly unfolded ASL by alphaA-crystallin | Homo sapiens |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
54 | - |
mid-point temperature transition 2 | Homo sapiens |
57 | - |
mid-point temperature transition 1 and 3 | Homo sapiens |
58 | - |
mid-point temperature transition 3, presence of alphaA-crystallin | Homo sapiens |
83 | - |
mid-point temperature transition 1, presence of alphaA-crystallin | Homo sapiens |
85 | - |
mid-point temperature transition 2, presence of alphaA-crystallin | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
metabolism | small heat shock protein, alphaA-crystallin, functions as a molecular chaperone, and enhances thermal stability of both delta-crystallin and ASL. Thermal unfolding of delta-crystallin or ASL in the presence of alphaA-crystallin follows a similar three-state model. A stable intermediate which retains about 30% alpha-helical structure is observed. Protection from thermal denaturation by alphaA-crystallin is by interaction with partly unfolded ASL to form high molecular weight heteroligomers. Aggregate formation of ASL is significantly reduced in the presence of alphaA-crystallin. The extent of protection of ASL at different ratios of alpahA-crystallin is described by hyperbolic curves, suggesting the preferential recognition of partly unfolded ASL by alphaA-crystallin | Homo sapiens |