Beta-peptides are known to be highly membrane-active.Many of sequences of the beta-peptides have been proved to have anti-microbial activity and antifungal activity. Most interestingly, the membrane activity of non-natural amino acids is known to be highly sequence-dependent. Part of our research on beta-peptides is focussed on understanding the sequence-dependence of the beta-peptides through atomistic simulation. Since, the atomistic treatment of membrane(lipid-bilayer) are computationally intensive, we are treating the membrane using an implicit description ( known as GBSW) while the beta-peptide is being treated atomistically using the recenty developed force-fields of beta-peptide in our group. The preliminary result is shown below. The picture on top shows the trajectory of a single beta-peptide at different times. We can see that starting from solvent phase, the beta-peptide goes to the interface quickly and remains attached there for the rest of the simulation. The figure in the bottom compares the extent of insertion of two isomers ( GA & Non-GA) of a particular beta-peptide sequence. We can clearly see that GA isomer goes further towards the membrane interior compared to Non-GA isomer.