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Sarah M. Tschampel
Researcher at University of Georgia
Publications - 7
Citations - 2060
Sarah M. Tschampel is an academic researcher from University of Georgia. The author has contributed to research in topics: Ligand (biochemistry) & Molecular dynamics. The author has an hindex of 7, co-authored 7 publications receiving 1748 citations. Previous affiliations of Sarah M. Tschampel include Massachusetts Institute of Technology.
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Journal ArticleDOI
GLYCAM06: a generalizable biomolecular force field. Carbohydrates.
Karl N. Kirschner,Austin B. Yongye,Sarah M. Tschampel,Jorge Gonzalez-Outeiriño,Charlisa R. Daniels,B. Lachele Foley,Robert J. Woods +6 more
TL;DR: It is demonstrated that deriving dihedral parameters by fitting to QM data for internal rotational energy curves for representative small molecules generally leads to correct rotamer populations in molecular dynamics simulations, and that this approach removes the need for phase corrections in the dihedral terms.
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Effects of glycosylation on peptide conformation: a synergistic experimental and computational study.
TL;DR: Computational and biophysical analyses reveal that the conformations of the peptide and alpha- and beta-linked glycopeptides are uniquely influenced by the attached saccharide, highlighting the value of computational approaches for probing the influence of attachedsaccharides on polypeptide conformation.
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The xenograft antigen bound to Griffonia simplicifolia lectin 1-B(4). X-ray crystal structure of the complex and molecular dynamics characterization of the binding site.
TL;DR: The first x-ray crystal structure of the xenograft antigen bound to a protein (GS-1-B(4)) is reported, and it is determined that GS-1,B( 4) recognizes the lowest energy conformation of the disaccharide.
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A hydration study of (1→4) and (1→6) linked α‐glucans by comparative 10 ns molecular dynamics simulations and 500‐MHz NMR
Francisco Corzana,Mohammed Saddik Motawia,Catherine Hervé du Penhoat,Serge Pérez,Sarah M. Tschampel,Robert J. Woods,Søren Balling Engelsen +6 more
TL;DR: In short, the older CHARMM‐based force field exhibited a more structured carbohydrate–water interaction leading to better agreement with the diffusional properties of the two compounds, whereas especially the α‐(1→6) linkage and the primary hydroxyl groups were inaccurately modeled.
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TIP5P-Consistent Treatment of Electrostatics for Biomolecular Simulations.
TL;DR: In this article, an atom-type specific lone-pair model is presented, which leads to the most optimal LP placement for each atom type, and, notably, results in reproduction of the lonepair description present in TIP5P.