Long-Range Intra-Protein Communication Can Be Transmitted by Correlated Side-Chain Fluctuations Alone
Figure 4
Distance dependence of mutual information in barstar and calmodulin.
Average excess mutual information as a function of distance between
atoms. For both (a) barstar and (b) calmodulin, we summed the values of
for all residue pairs within several inter-residue distance ranges and then divided by the number of such pairs. Results are shown for various subsets of atomic interactions: S indicates repulsive sterics, IS indicates implicit solvent, LJ indicates the Lennard-Jones interaction, and HBSB indicates the hydrogen bonding and salt-bridge interactions. See Methods for binning details.