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>