10.1371/journal.pntd.0003661.g005 Sandip Kumar Nandi Sandip Kumar Nandi Ayon Chakraborty Ayon Chakraborty Alok Kumar Panda Alok Kumar Panda Sougata Sinha Ray Sougata Sinha Ray Rajiv Kumar Kar Rajiv Kumar Kar Anirban Bhunia Anirban Bhunia Ashis Biswas Ashis Biswas Enhancement of chaperone activity of <i>M</i>. <i>leprae</i> HSP18 induced by ATP and its non-hydrolysable analog, ATP-γS. Public Library of Science 2015 antigenic proteins act chaperone function heat shock protein Comparative sequence alignment Small Heat Shock Protein HSP 18 Molecular docking studies Mycobacterium leprae bacilli sequence 49 KADSLDIDIE 58 leprae HSP 18 18 kDa antigen ATP triggers exposure leprae HSP 18. ATP perturbs surface plasmon resonance measurement 2015-03-26 04:46:04 Figure https://plos.figshare.com/articles/figure/_Enhancement_of_chaperone_activity_of_M_leprae_HSP18_induced_by_ATP_and_its_non_hydrolysable_analog_ATP_S_/1357689 <p>Thermal aggregation of 0.06 mg/ml CS at 43°C <b>(panel A)</b> and DTT-induced aggregation of 0.05 mg/ml lysozyme at 37°C <b>(panel B)</b> in the absence or presence of different HSP18 preparations. Trace 1:Client protein (CP) alone; Trace 2: CP + 1 mM ATP; Trace 3: CP + 1 mM ATP-γS; Trace 4: CP+ HSP18; Trace 5: CP + HSP18 preincubated with 1 mM ATP; Trace 6: CP + HSP18 preincubated with 1 mM ATP-γS. Each data point is the average of triplicate measurements. <b>Panels C and D</b> represents the percent protection ability of different HSP18 preparations against CS and lysozyme aggregation. The chaperone:client protein ratio was 1:1 (w/w) for CS and lysozyme aggregation assays. Data are the means ± standard deviation from triplicate measurements. **<i>p</i>< 0.005 and ***<i>p</i><0.0005.</p>