Article
The transmembrane domain of Neu in a lipid bilayer: molecular dynamics simulations.
European biophysics journal : EBJ - 1 Nov 2004
van der Ende Bryan M, Sharom Frances J, Davis James H
Abstract excerpt
The results of full-atom molecular dynamics simulations of the transmembrane domains (TMDs) of both native, and Glu664-mutant (either protonated or unprotonated) Neu in an explicit fully hydrated dimyristoylphosphatidylcholine (DMPC) lipid bilayer are presented. For the native TMD peptide, a 10.05 ns trajectory was collected, while for the mutant TMD peptides 5.05 ns trajectories were collected for each. The...
Topics
- Amino Acid Substitution
- Cell Membrane
- Computer Simulation
- Dimyristoylphosphatidylcholine
- Glutamine
- Kinetics
- Lipid Bilayers
- Membrane Fluidity
- Models, Chemical
- Models, Molecular
- Motion
- Mutation
- Protein Conformation
- Protein Structure, Tertiary
- Receptor, ErbB-2
- Structure-Activity Relationship