Comparison of the atomic fluctuations per residue for the last 30 ns of the simulation. The RMSF values for each monomer of the homodimer and heterodimer are displayed in (A) and (B), respectively. Asterisks (*) indicate the mutated residues of the TWIST1 monomer. The b-factors represented in cartoon form for the homo- and heterodimers (the wt and mutants) are displayed in (C) and (D), respectively. The most fluctuating residues are colored in red (terminal residues), and the remainder of the dimer is in light blue (the most stable), in accordance with the observed fluctuations observed. Å – angstrom (10-10 m);ns – nanoseconds (10-9 s).
Maia et al. BMC Bioinformatics 2012 13:184 doi:10.1186/1471-2105-13-184