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. Author manuscript; available in PMC: 2012 Apr 15.
Published in final edited form as: J Mol Biol. 2011 Feb 17;407(5):716–730. doi: 10.1016/j.jmb.2011.02.001

Figure 1. Conformation of the nucleotide-binding pocket as function of temperature monitored by FRET between dmantADP and MV FlAsH.

Figure 1

The emission of 0.5 µM MV FlAsH (A) or acto-MV FlAsH (B) was measured in the presence of increasing concentrations of dmantADP at 4 and 35 °C. The FRET efficiency was monitored by the enhancement in the acceptor fluorescence and the maximum FRET efficiency was determined by fitting the data to a hyperbolic binding function. Error bars represent the standard deviation from at least three separate experiments done with three different protein preparations.