R
Rick L. Ornstein
Researcher at Pacific Northwest National Laboratory
Publications - 68
Citations - 2184
Rick L. Ornstein is an academic researcher from Pacific Northwest National Laboratory. The author has contributed to research in topics: Ab initio & Active site. The author has an hindex of 29, co-authored 68 publications receiving 2123 citations. Previous affiliations of Rick L. Ornstein include Environmental Molecular Sciences Laboratory & Battelle Memorial Institute.
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A Theoretical Study of the Structures of Flavin in Different Oxidation and Protonation States
Ya-Jun Zheng,Rick L. Ornstein +1 more
TL;DR: In this paper, the authors used molecular orbital theory to investigate the structure of flavin in different oxidation and protonation states using lumiflavin as a model compound, and they showed that oxidized flavin is planar and reduced flavin H3Flred has a ring puckering angle of 27.3° along the N5 and N10 axis.
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Effect of periodic box size on aqueous molecular dynamics simulation of a DNA dodecamer with particle-mesh Ewald method
O.N. de Souza,Rick L. Ornstein +1 more
TL;DR: Based on a comparison of RMSDs and curvature for this single DNA dodecamer sequence, the larger two box sizes do not appear to afford any extra benefit over the smallest box, which is similar to the box size currently chosen by most workers in the field.
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Reaction Pathways and Energy Barriers for Alkaline Hydrolysis of Carboxylic Acid Esters in Water Studied by a Hybrid Supermolecule-Polarizable Continuum Approach
TL;DR: In this article, solvent effects and energy barriers for base-catalyzed hydrolysis of two representative alkyl esters in aqueous solution were determined using a hybrid supermolecule-polarizable continuum approach.
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A Molecular Dynamics and Quantum Mechanics Analysis of the Effect of DMSO on Enzyme Structure and Dynamics: Subtilisin
Ya-Jun Zheng,Rick L. Ornstein +1 more
TL;DR: In this article, a 745-ps molecular dynamics simulation of the enzyme subtilisin Carlsberg in a periodic box of DMSO was performed and the starting coordinates for subtilis and crystallographic waters were taken from the aqueous X-ray crystal structure.
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Binding free energy calculations for P450cam-substrate complexes
Mark D. Paulsen,Rick L. Ornstein +1 more
TL;DR: A recently proposed semi-empirical method for calculating binding free energies was used to examine the binding of a variety of substrates to cytochrome P450cam, and the ability of this method to predict the effect of active site mutations was examined.