Correction to Addition of αA-Crystallin Sequence 164–173 to a Mini-Chaperone DFVIFLDVKHFSPEDLT Alters the Conformation but Not the Chaperone-like Activity
نویسندگان
چکیده
Received: May 12, 2014 Published: May 22, 2014 Figure 5. Aggregations of denaturing proteins in the presence of miniαA-chaperone or chimeric mini-chaperone (CP1). (A) Heatand EDTA-induced ADH (5 μM) aggregation in the presence of mini-αA (40 μM) or mini-αA (Δ87−88, 40 μM) at 37 °C. (B) Heat-induced citrate synthase (4 μM) aggregation assay at 43 °C in the presence of mini-αA (40 μM) or CP1 (40 μM). (C) ADH (5 μM) aggregation in the presence of mini-αA (40 μM) or CP1 (40 μM). (D) Chaperonelike activity of mini-αA or CP1 peptide toward DDT-induced aggregation of LA at 37 °C. Addition/Correction
منابع مشابه
Addition of αA-Crystallin Sequence 164–173 to a Mini-Chaperone DFVIFLDVKHFSPEDLT Alters the Conformation but Not the Chaperone-like Activity
It has been shown that αA-mini-chaperone, a peptide representing the chaperone binding site in αA-crystallin, prevents destabilized protein aggregation. αA-Mini-chaperone has been shown to form amyloid fibrils. This study was undertaken to improve the stability of αA-mini-chaperone while preserving its anti-aggregation activity by fusing the flexible and solvent-exposed C-terminal 164-173 regio...
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