## 3 Results and Discussion
Finally, the net transfer entropy was further decomposed and replotted for each of the 20 residue types, as depicted in Figure 7, using a bar plot to display the average net transfer entropy where the entropy source (donor) and sink (acceptor) residues can be identified by their positive and negative values, respectively. Corresponding plots that display net transfer entropy for a pair of residue types such as entropy donor versus entropy acceptor are provided in Supplementary Figure S3. Further categorization of residues as hydrophobic and polar clearly demonstrated the dominancy of polar residues as entropy donors, whereas hydrophobic ones were most often identified as entropy acceptors. In the case of backbone rotation angles only, _Trp_ appeared as the strongest entropy acceptor site in both MD runs, whereas _His_ displayed the highest positive average net transfer entropy (See Figure 7a). Exceptionally, _Gly_ residue with no side-chain atoms appeared as a strong entropy donor site. Figure 6: Net transfer entropy from residue \(i\) to residue \(j\) (see Equation (8)) for two independent MD runs using (**a**) backbone torsion angles, (\(\phi\), \(\psi\)), (**b**) backbone torsion angles, (\(\phi\), \(\psi\)) and the first side-chain torsion angle (\(\chi_{1}\) ) and (**c**) all possible side-chain torsion angles \(\chi_{k},\ k=1,2,3,4\). Color code for (**a**,**b**): no display for \(\langle netTE\rangle\leq 4\); magenta for \(4<\langle netTE\rangle\leq 8\), green for \(8<\langle netTE\rangle\leq 12\) and red for \(12>\langle netTE\rangle\). Noticeably, the close correspondence between polarity/hydrophobicity and donor/acceptor features was the strongest when all side-chain torsion angles were considered in transfer entropy calculations (See Figure 7c). Most hydrophobic residues, except _Met_, which is mostly located at the protein's core region, displayed strong entropy acceptor characteristics, especially _Pro_, with the lowest average net transfer entropy value of \(-7.38\) calculated so far. Furthermore, on the polar side, _Arg_ and _Lys_, with a total of four side-chain torsion angles, displayed the highest entropy values exceeding +10. Upon incorporating the first side-chain torsion angle (\(\chi_{1}\)) along with two backbone torsion angles, the profile changed slightly, yet the dominancy of polar residues as entropy donor sites persisted (See Figure 7b). Three polar residues, _Lys_, _Glu_, _and_\(\mathit{Gln}\), displayed the highest positive transfer entropy values in both runs. Interestingly, the two polar _Ser_, _Thr_, and the hydrophobic _Tyr_, which all contain a hydroxyl group in their side-chain, displayed entropy sink (acceptor) features. Figure 7: Net transfer entropy averaged for each residue type categorized as either hydrophobic (blue tones) or polar (pink tones). The number of side-chain torsion angles \(k\) indicated at the top of each bar is determined for both MD runs using (**a**) backbone torsion angles, (\(\phi\), \(\psi\)), (**b**) backbone torsion angles, (\(\phi\), \(\psi\)) and the first side-chain torsion angle (\(\chi_{1}\) ) and (**c**) all possible side-chain torsion angles \(\chi_{k}\), \(k=1,2,3,4\).