Article
C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine alphaB-crystallin.
Biochemical and biophysical research communications - 20 Sept 2002
Liao Jiahn-Haur, Lee Jiahn-Shing, Chiou Shyh-Horng
Abstract excerpt
The carboxyl-terminal segment of alpha-crystallin, a major lens protein of all vertebrates, has a short and flexible peptide extension of about 20 amino acid residues that are very susceptible to proteolytic truncation and modifications under physiological conditions. To investigate its role in crystallin aggregation and chaperone-like activity, we constructed a mutant of porcine alphaB-crystallin with C-terminal...
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