TY - DATA T1 - Dataset for: Curved or linear: Predicting the 3-dimensional structure of α-helical antimicrobial peptides in an amphipathic environment PY - 2019/12/03 AU - Glen van den Bergen AU - Martin Stroet AU - Bertrand Caron AU - David Poger AU - Alan E. Mark UR - https://wiley.figshare.com/articles/dataset/Dataset_for_Curved_or_linear_Predicting_the_3-dimensional_structure_of_-helical_antimicrobial_peptides_in_an_amphipathic_environment/11299052 DO - 10.6084/m9.figshare.11299052.v1 L4 - https://ndownloader.figshare.com/files/20025902 L4 - https://ndownloader.figshare.com/files/20025905 KW - antimicrobial peptides KW - hydrophobic moment KW - amphipathicity KW - membrane KW - curvature KW - α-helix KW - Biophysics KW - Synthetic Biology KW - Biochemistry KW - Plant Biology KW - Virology KW - Cell Development, Proliferation and Death KW - Computational Biology KW - Immunology KW - Neuroscience KW - Receptors and Membrane Biology KW - Molecular Biology KW - Evolutionary Biology KW - Signal Transduction KW - Cancer Cell Biology KW - Systems Biology KW - Structural Biology N2 - α-Helical membrane-active antimicrobial peptides (AMPs) are known to act via a range of mechanisms including the formation of barrel-stave and toroidal pores, and the micellisation of the membrane (carpet mechanism). Different mechanisms imply the peptides adopt different 3D-structures when bound at the water-membrane interface, a highly amphipathic environment. Here an evolutionary algorithm is used to predict the 3D-structure of a range of α-helical membrane-active AMPs at the water-membrane interface by optimising amphipathicity. This amphipathic structure prediction (ASP) is capable of distinguishing between curved and linear peptides solved experimentally, potentially allowing the activity and mechanism of action of different membrane-active AMPs to be predicted. The ASP algorithm is accessible via a web interface at http://atb.uq.edu.au/asp/. ER -