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Correction to Addition of αA-Crystallin Sequence 164–173 to a Mini-Chaperone DFVIFLDVKHFSPEDLT Alters the Conformation but Not the Chaperone-like Activity
Author(s) -
Murugesan Raju,
Puttur Santhoshkumar,
Leike Xie,
K. Krishna Sharma
Publication year - 2014
Publication title -
biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.43
H-Index - 253
eISSN - 1520-4995
pISSN - 0006-2960
DOI - 10.1021/bi500563d
Subject(s) - notice , altmetrics , citation , computer science , chaperone (clinical) , information retrieval , social media , world wide web , medicine , political science , pathology , law
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

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