Fig. 5. Dimerization preventing the E49Q D154N N-Ras variant. (A) Schematic summary of the key dimer interactions (Table S6†) obtained from MD simulations (Table S7†) suggesting E49 and D154 as promising candidates for dimer preventing mutations. (B) FRET measurements of the lipidated membrane-bound N-Ras E49Q D154N variant confirm that mutations of E49 and D154 prevent the dimer formation as no observable FRET signals were detected compared to N-Ras WT (C). The computationally predicted N-Ras dimer interface is experimentally validated.