%0 Figure %A Kumar Nandi, Sandip %A Chakraborty, Ayon %A Kumar Panda, Alok %A Ray, Sougata Sinha %A Kumar Kar, Rajiv %A Bhunia, Anirban %A Biswas, Ashis %D 2015 %T Enhancement of chaperone activity of M. leprae HSP18 induced by ATP and its non-hydrolysable analog, ATP-γS. %U 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 %R 10.1371/journal.pntd.0003661.g005 %2 https://plos.figshare.com/ndownloader/files/1990936 %K antigenic proteins act %K chaperone function %K heat shock protein %K Comparative sequence alignment %K Small Heat Shock Protein %K HSP 18 %K Molecular docking studies %K Mycobacterium leprae bacilli %K sequence 49 KADSLDIDIE 58 %K leprae HSP 18 %K 18 kDa antigen %K ATP triggers exposure %K leprae HSP 18. ATP perturbs %K surface plasmon resonance measurement %X

Thermal aggregation of 0.06 mg/ml CS at 43°C (panel A) and DTT-induced aggregation of 0.05 mg/ml lysozyme at 37°C (panel 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. Panels C and D 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. **p< 0.005 and ***p<0.0005.

%I PLOS Neglected Tropical Diseases