Kumar Nandi, Sandip Chakraborty, Ayon Kumar Panda, Alok Ray, Sougata Sinha Kumar Kar, Rajiv Bhunia, Anirban Biswas, Ashis Enhancement of chaperone activity of <i>M</i>. <i>leprae</i> HSP18 induced by ATP and its non-hydrolysable analog, ATP-γS. <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> 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
    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
10.1371/journal.pntd.0003661.g005