Fig. 6: Effects of nucleotide variation on substrate translocation.
From: Nonequilibrium chemomechanical transduction of ATP-driven protein unfolding in the 26S proteasome
a The coupling between resistance of substrate and the number of bound ADPs within the AAA-ATPase motor. The simulations were conducted at an ATP concentration of 1 mM. b Normalized translocation rates plotted as a function of the [ATP\(\gamma\)S]/[ATP] ratio in human and yeast proteasome and E. coli ClpX, obtained from experiments and our simulations. The rates are normalized by the translocation rate without the inhibition of ATPγS. The experiment data are from refs. 28,33,38.
