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R. Sharon

Researcher at Weizmann Institute of Science

Publications -  10
Citations -  1509

R. Sharon is an academic researcher from Weizmann Institute of Science. The author has contributed to research in topics: Molecular dynamics & Thermus thermophilus. The author has an hindex of 8, co-authored 10 publications receiving 1462 citations. Previous affiliations of R. Sharon include Stanford University.

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Calibration and Testing of a Water Model for Simulation of the Molecular Dynamics of Proteins and Nucleic Acids in Solution

TL;DR: In this paper, a flexible three-centered water model (F3C) is proposed for simulation of biological macromolecules in solution, and the model is further tested by comparing calculated energetic, structural, and dynamic properties of liquid water, at several temperatures and pressures, with experiment.
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Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution

TL;DR: In this article, the complete set of energy parameters used in the ENCAD (Energy Calculation and Dynamics) simulation program is presented, including the form of the potential, which has been designed for efficient simulation of trajectories of macromolecules in solution.
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Accurate simulation of protein dynamics in solution.

TL;DR: Simulation of the molecular dynamics of a small protein, bovine pancreatic trypsin inhibitor, was found to be more realistic when water molecules were included than when in vacuo, using atom-centered forces and classical mechanics.
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A milestone in ribosomal crystallography: the construction of preliminary electron density maps at intermediate resolution

TL;DR: The surface of these ribosomal particles is being characterized and procedures are being developed for quantitative detachment of selected Ribosomal proteins and for their incorporation into core particles, for their crystal production in large quantities.
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Characterization and preliminary crystallographic studies on large ribosomal subunits from Thermus thermophilus.

TL;DR: Crystallographic analysis of the various members of this series should provide information for investigating the conformational changes that take place upon the association of ribosomes from their subunits as well as upon binding of non-ribosomal components that participate in protein biosynthesis.