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. Author manuscript; available in PMC: 2016 Jul 21.
Published in final edited form as: Biochemistry. 2015 Jul 10;54(28):4374–4390. doi: 10.1021/acs.biochem.5b00018

Figure 6. Residuals of the average number of contacts made by transmembrane helices of P-glycoprotein with daunorubicin for each independent simulation.

Figure 6

These graphs are similar to those presented in Figure 5, except that the number of contacts at each point of progression in the six individual simulations with daunorubicin was subtracted from the average number of contacts at that point in the simulations. The graphs are intended to highlight the variability of contacts made between each transmembrane helix with daunorubicin as P-gp moved from open inside to open outside conformations. Results from six independent simulations are shown.