Skip to main content
. 2012 Jun 4;7(6):e38259. doi: 10.1371/journal.pone.0038259

Figure 2. Effect of disease-related protein modifications on the rate of Ca2+ dissociation from the Tn complex.

Figure 2

Panel A shows the time courses of the increase in IAANS fluorescence as Ca2+ was removed by EGTA from control Inline graphic, and the DCM mutants, TnI K36Q Inline graphic, TnT R131W Inline graphic, TnT R141W Inline graphic, TnT R205L Inline graphic and TnT ΔK210 Inline graphic. Panel B shows the time courses of the increase in IAANS fluorescence as Ca2+ was removed by EGTA from control Inline graphic, and the HCM mutants, TnT R92Q Inline graphic and TnI S166F Inline graphic. Panel C shows the time courses of the increase in IAANS fluorescence as Ca2+ was removed by EGTA from control Inline graphic, and the RCM mutants, TnI D190H Inline graphic and TnI R192H Inline graphic. Panel D shows the time courses of the increase in IAANS fluorescence as Ca2+ was removed by EGTA from control Inline graphic and ischemic related truncated TnI (1-192) Inline graphic. All Inline graphic complexes consist of the full length Tn subunits of Inline graphic, TnI and TnT, except for ischemic related truncated TnI (1-192). The disease related modification is either in TnI or TnT, in either case, the other protein (TnT or TnI) was wild type. Data traces (an average of 3 to 5 individual traces collected at least 10 times) were fit with a single exponential equation to calculate the kinetic rates. The data traces have been staggered and normalized for clarity.