Fig. 6
From: Genetic and molecular dynamics analysis of two variants of the COL4A5 gene causing Alport syndrome
Protein molecular dynamics simulation of the α5(IV). (A) The conformation of the wild-type α5(IV), mute1-α5(IV), and mute2-α5(IV) chains was analyzed using molecular dynamics simulations over a period of 90 ns. (B) During a 90 ns period, the RMSD of the chains wild-α5(IV), mute1-α5(IV), and mute2-α5(IV) was analyzed. (C) The RMSF was calculated for every amino acid residue present in the wild-α5(IV), mute1-α5(IV), and mute2-α5(IV) chains over a time period ranging from 80 ns to 90 ns. (D) During a 100 ns simulation, the secondary structure counts of the wild-type α5(IV), mute1-α5(IV), and mute2-α5(IV) chains were determined