Molecular dynamics simulation provides the methodology for detailed microscopic modeling on the molecular scale and captures the atomic resolution behavior of biological systems on timescales spanning 12 orders of magnitude. It is a useful partner to biological experiment, which has the spatial and temporal resolution limits of current experimental techniques. In recent years, molecular dynamics simulation has making rapid progress since advances in computer hardware and atomistic simulation algorithms.
Membrane proteins is responsible for interactions of cells with their surrounding environment and also constitute about 50% of current drug targets, but its experimental characterization of structural dynamics is still challenging. Antimicrobial peptides are found as part of immune system of many organisms to against invading bacteria and other microorganisms by disturbing membrane permeation properties, however the exact mechanism is not fully understood at present and it is difficult to map details of peptide-membrane interactions using experimental techniques. Molecular dynamics simulation is a promising methodology to study the process of membrane protein and antimicrobial peptide interacting with lipid bilayer membranes and their functional dynamics in native state. This research is aimed at the area described above, for the purpose of making further progress.
Prof. Wei and Prof. Jakob Ulmschneider have the similar interesting in molecular dynamics simulation, and they have succeeded in revealing the mechanism of some antimicrobial peptides partitioning, folding and assembly in lipid bilayer membranes via unbiased atomic detail microsecond molecular dynamics simulation.