Skip to main content
. Author manuscript; available in PMC: 2014 Jun 20.
Published in final edited form as: J Phys Chem B. 2013 Jun 5;117(24):7283–7291. doi: 10.1021/jp403207c

Figure 3.

Figure 3

The difference in the first order entropy (ΔS1) for each amino acid in m23-β1AR and wt-β1AR. A. ΔS1 plotted against the position in the amino acid sequence. Filled black circles show the location of the 6 thermostabilizing mutations in m23-β1AR. B. The difference in first order entropy between wt-β1AR and m23-β1AR is depicted on a cartoon of the m23-β1AR structure: regions in blue have lower entropy in m23-β1AR compared to wt-β1AR, while regions in red have higher entropy. The side chains of thermostabilizing residues are shown as black spheres.