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Literature summary for 4.3.2.1 extracted from

  • Chen, Y.H.; Lee, M.T.; Cheng, Y.W.; Chou, W.Y.; Yu, C.M.; Lee, H.J.
    Distinct interactions of alphaA-crystallin with homologous substrate proteins, delta-crystallin and argininosuccinate lyase, under thermal stress (2011), Biochimie, 93, 314-320.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Subunits

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 [°C]

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

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