title: Data supporting beta-amyloid dimer structural transitions and protein-lipid interactions on asymmetric lipid bilayer surfaces using MD simulations on experimentally derived NMR protein structures.
abstract: This data article supports the research article entitled "Maximally Asymmetric Transbilayer Distribution of Anionic Lipids Alters the Structure and interaction with Lipids of an Amyloidogenic Protein Dimer Bound to the Membrane Surface" [1]. We describe supporting data on the binding kinetics, time evolution of secondary structure, and residue-contact maps of a surface-absorbed beta-amyloid dimer protein on different membrane surfaces. We further demonstrate the sorting of annular and non-annular regions of the protein/lipid bilayer simulation systems, and the correlation of lipid-number mismatch and surface area per lipid mismatch of asymmetric lipid membranes.
authors.affiliation: Department of Physics, University of Texas at Austin, Austin, TX 78712, USA.
authors.forename: Sara Y
authors.initials: SY
authors.lastname: Cheng
authors.affiliation: Department of Chemical Engineering, Texas Tech University, Lubbock, TX 79409, USA.
authors.forename: George
authors.initials: G
authors.lastname: Chou
authors.affiliation: Department of Chemical Engineering, Texas Tech University, Lubbock, TX 79409, USA.
authors.forename: Creighton
authors.initials: C
authors.lastname: Buie
authors.affiliation: Department of Chemical Engineering, Texas Tech University, Lubbock, TX 79409, USA.
authors.forename: Mark W
authors.initials: MW
authors.lastname: Vaughn
authors.affiliation: Department of Computer Science, Trinity University, San Antonio, TX 78212, USA.
authors.forename: Campbell
authors.initials: C
authors.lastname: Compton
authors.affiliation: Department of Physics, Texas Tech University, Lubbock, TX 79409, USA; Department of Physics and Astronomy, Trinity University, San Antonio, TX 78212, USA.
authors.forename: Kwan H
authors.initials: KH
authors.lastname: Cheng
keywords: Asymmetric lipid membranes; Beta-Amyloid; Protein aggregation; Protein structure on surfaces; Protein–lipid interactions