Correction to Addition of αA-Crystallin Sequence 164–173 to a Mini

ACS AuthorChoice - This is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article...
0 downloads 0 Views 376KB Size
Addition/Correction pubs.acs.org/biochemistry

Open Access on 05/22/2015

Correction to Addition of αA-Crystallin Sequence 164−173 to a Mini-Chaperone DFVIFLDVKHFSPEDLT Alters the Conformation but Not the Chaperone-like Activity Murugesan Raju, Puttur Santhoshkumar, Leike Xie, and K. Krishna Sharma* Biochemistry 2014, 53 (16), 2615−2623. DOI: 10.1021/bi4017268

Figure 5. Aggregations of denaturing proteins in the presence of miniαA-chaperone or chimeric mini-chaperone (CP1). (A) Heat- and 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.

Received: May 12, 2014 Published: May 22, 2014 © 2014 American Chemical Society

3521

dx.doi.org/10.1021/bi500563d | Biochemistry 2014, 53, 3521−3521