Figure 3

(A) Circular-Dichroic spectra of Rv1694. Rv1694-6-histidine tag fusion protein (0.5 mg/ml in 10 mM Na-Phosphate buffer, pH 7.4) was used for obtaining CD spectra. CD data, as interpreted from Yang's calculation, shows that Rv1694 has 23% α-helix, 32.8% β-sheet, 7.7% turns and 36.5% random coil. (B) Model of Rv1694: Model of Rv1694 was built using the putative hemolysin from Streptococcus thermophilus, using 3HP7.pdb as template with the help of Swiss Model Server [33]. The Rv1694 has a typical fold of a ribosomal RNA polymerase consisting of 7 β-sheets surrounded by 5 α-helices. Please note that the amino acids 246-268(QTD...EGP) are not present in the depicted model. The white arrow points the region containing basic amino acids between the domains susceptible to proteases like trypsin/Proteinase K.