Long-Range Intra-Protein Communication Can Be Transmitted by Correlated Side-Chain Fluctuations Alone

doi:10.1371/journal.pcbi.1002168

Long-Range Intra-Protein Communication Can Be Transmitted by Correlated Side-Chain Fluctuations Alone

Figure 3

Mutual information of residue pairs in calmodulin.

The mutual information, , associated with side-chain fluctuations of residue pairs in calmodulin. Plots (b)–(f) display the mutual information signal∶noise ratio, (upper left triangles) and the excess mutual information (lower right triangles), as indicated in (a). The - and -axes run over labels, and respectively, of residues in the amino acid sequence, excluding those lacking rotameric freedom in our model. Scale bars for the signal∶noise ratio and the excess mutual information are presented on the top and bottom left, respectively. Results are shown for the following combinations of interactions: (b) repulsive sterics (S), (c) implicit solvent (IS) (d) Lennard-Jones (LJ) interaction comprising repulsive sterics and van der Waals attractions, (e) hydrogen bonding and salt-bridges (HBSB), and (f) the full potential (LJ+HBSB+IS). Residue 30K, which we scrutinize in detail later (see Fig. 5), is highlighted in (f) for reference.

doi: https://doi.org/10.1371/journal.pcbi.1002168.g003