Thermodynamics Behavior of Transmembrane Protein

In continue with our recent studies on the claudins as a class of blood-brain barrier (BBB) and very good target for the specific channel of the drug delivery systems, in this part we are going to focus on the dynamic behavior and thermodynamic stability of the of claudin embedded in DMPC membrane, in 3 different temperature by RMSD. About twenty different claudins are recognized until now which are classified into two part, classical and nonclassified protein. By detailed researches on (BBB), it has been reported that (BBB) is constructed mostly by claudin-5 which is an integral protein. It has been driven from recent studies that accuracy of homology model with the atomistic MD simulations, showed how the hydrophobic residues provide structural stability to the monomeric structure and effect on drug transport from blood to brain MD simulations were performed using GROMACS. The lowest energy model of the protein was embedded in a DMPC bilayer for simulation with explicit TIP3 water model three different temperature and 0.15 M, KCl solution. The simulations used the CHARMM36 force field parameters for proteins, lipid, and water. As an acknowledgment to previous studies flexible regions e.g. Large loops unwound termini can cause large contributions to RMSD and for another stabilitiy Cα RMSF which is a measure of the local chain flexibility shows more fluctuations for residues which are in direct contact with solutions as an example (r:30-47).