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Force-Field Induced Bias in the Structure of A beta(21-30): A Comparison of OPLS, AMBER, CHARMM, and GROMOS Force Fields
Journal article   Peer reviewed

Force-Field Induced Bias in the Structure of A beta(21-30): A Comparison of OPLS, AMBER, CHARMM, and GROMOS Force Fields

Micholas Dean Smith, J. Srinivasa Rao, Elizabeth Segelken, Luis Cruz and Michael D Smith
Journal of chemical information and modeling, v 55(12), pp 2587-2595
01 Dec 2015
PMID: 26629886

Abstract

Chemistry Chemistry, Medicinal Chemistry, Multidisciplinary Computer Science Computer Science, Information Systems Computer Science, Interdisciplinary Applications Life Sciences & Biomedicine Pharmacology & Pharmacy Physical Sciences Science & Technology Technology
In this work we examine the dynamics of an intrinsically disordered protein fragment of the amyloid beta, the A beta(21-30), under seven commonly used molecular dynamics force fields (OPLS-AA, CHARMM27-CMAP, AMBER99, AMBER99SB, AMBER99SB-ILDN, AMBER03, and GROMO-S53A6), and three water models (TIP3P, TIP4P, and SPC/E). We find that the tested force fields and water models have little effect on the measures of radii of gyration and solvent accessible surface area (SASA); however, secondary structure measures and intrapeptide hydrogen-bonding are significantly modified, with AMBER (99, 99SB, 995B-ILDN, and 03) and CHARMM22/27 force-fields readily increasing helical content and the variety of intrapeptide hydrogen bonds. On the basis of a comparison between the population of helical and beta structures found in experiments, our data suggest formation of helical structure might be a better choice to model the A beta(21-30) peptide.

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Collaboration types
Domestic collaboration
Web of Science research areas
Chemistry, Medicinal
Chemistry, Multidisciplinary
Computer Science, Information Systems
Computer Science, Interdisciplinary Applications
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