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Katrine Kirkeby Skeby (a), Emad Tajkhorshid (b) and Birgit Schiøtt (a) (a.Department of Chemistry, iNANO, and inSPIN centers, Aarhus University, b. Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois.)Molecular dynamics simulation is a unique method, in having high resolution in space as well as time. We have utilized this to investigate a molecular system at a level of detail otherwise unattainable. Amyloid proteins are linked to severe diseases such as Alzheimer’s Disease and Type 2 Diabetes (T2D). Protein aggregates are deposited in disease specific tissues, where amyloid aggregation is cytotoxic. Lipid membranes accelerate the formation of the cytotoxic aggregates. These properties make the membrane-peptide interactions difficult to study experimentally. The membrane bound conformation of amylin which is linked to T2D, has not yet been determined. Here, we use a highly mobile membrane model to capture the binding events of amylin. In agreement with experiments, we find the N-terminal to have α-helical structure and the C-terminal to be highly flexible without well-defined secondary structure. Attraction to the negative membrane is mediated by the positive residues in the N-terminal. These simulations agree well with the available experimental data, and provide a unique insight into the details of amylin-membrane interactions not feasible with experiments.