Figure 7
Mutation of leucine 773 to proline leads to disruption of the hydrophobic residue network at GR’s terminus. (A) The hydrogen bonding network around leucine 773. (Β–D) Hydrogen bond pairs, as indicated in the plots, between GR’s C-terminus and H10 residues exhibit higher distances in GR L773P MD simulations (n = 2, t = 100 ns). (E) The hydrophobic interaction network around leucine 773 as visualized with BIOVIA discovery studio shows how the neighboring to the mutation residues, Phe774 and Leu772 are in the epicenter of extensive hydrophobic interactions with GR elements in H10, β-sheet 2, H9 and H8.
