Figure_2.tif (3.99 MB)

Effect of ribosome and domain V RNA on refolding of lysozyme.

Download (0 kB)
posted on 07.05.2014, 03:39 by Bani Kumar Pathak, Surojit Mondal, Amar Nath Ghosh, Chandana Barat

A) Reduced-denatured lysozyme (2 µM) was refolded for 16 h in redox buffer (Material and methods). Bar diagram shows the reactivation yields in absence of the chaperone (Self) and in presence of bDV RNA, bDV RNA+Rnase. Reactivation yields in presence of 70S ribosome (70S) and Proteinase K treated and phenol extracted ribosome that was digested with RNase (70S ribosome+Rnase) are also shown. B) Time course of change in turbidity at 450 nm of reduced-denatured lysozyme (2 µM ) upon dilution of denaturant into the non-redox buffer (Material and methods), in absence of chaperone (-▪-), in presence of bDV RNA (-•-), in presence of mDV RNA (-▴-) and 70S ribosome (-Δ-). C) Negative staining transmission electron micrographs of reduced-denatured lysozyme under refolding condition in absence (i) and in presence of bDV RNA (ii). Molar ratio of BCAII to bDV RNA is 1∶1.