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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

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...

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Autores principales: Cheng, Sara Y., Chou, George, Buie, Creighton, Vaughn, Mark W., Compton, Campbell, Cheng, Kwan H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4802547/
https://www.ncbi.nlm.nih.gov/pubmed/27054174
http://dx.doi.org/10.1016/j.dib.2016.03.015
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author Cheng, Sara Y.
Chou, George
Buie, Creighton
Vaughn, Mark W.
Compton, Campbell
Cheng, Kwan H.
author_facet Cheng, Sara Y.
Chou, George
Buie, Creighton
Vaughn, Mark W.
Compton, Campbell
Cheng, Kwan H.
author_sort Cheng, Sara Y.
collection PubMed
description 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.
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spelling pubmed-48025472016-04-06 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 Cheng, Sara Y. Chou, George Buie, Creighton Vaughn, Mark W. Compton, Campbell Cheng, Kwan H. Data Brief Biochemistry, Genetics and Molecular Biology 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. Elsevier 2016-03-10 /pmc/articles/PMC4802547/ /pubmed/27054174 http://dx.doi.org/10.1016/j.dib.2016.03.015 Text en © 2016 Published by Elsevier Inc. http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Biochemistry, Genetics and Molecular Biology
Cheng, Sara Y.
Chou, George
Buie, Creighton
Vaughn, Mark W.
Compton, Campbell
Cheng, Kwan H.
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
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
title_full 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
title_fullStr 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
title_full_unstemmed 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
title_short 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
title_sort 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
topic Biochemistry, Genetics and Molecular Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4802547/
https://www.ncbi.nlm.nih.gov/pubmed/27054174
http://dx.doi.org/10.1016/j.dib.2016.03.015
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