Fig. 7
From: Genetic and molecular dynamics analysis of two variants of the COL4A5 gene causing Alport syndrome
Protein molecular dynamics simulation of the α345(IV) trimer. (A) Molecular dynamics simulations were employed to investigate the conformation of the triple chains of wild-α345(IV), mute1-α345(IV), and mute2-α345(IV) over a period of 90 ns. (B) The RMSD of the triple chains comprising wild-α345(IV), mute1-α345(IV), and mute2-α345(IV) was evaluated over a period of 90 ns. (C) The RMSF was calculated for every amino acid residue within the triple chains of wild-α345(IV), mute1-α345(IV), and mute2-α345(IV) over a time period ranging from 80 ns to 90 ns. (D) During a 100 ns simulation, the secondary structure counts were determined for the triple chains of wild-α345(IV), mute1-α345(IV), and mute2-α345(IV)