Jeremy Smith Governor's Chair and Director, UT-ORNL Center for Molecular Biophysics Contact SMITHJC@ORNL.GOV All Publications Force-Field Development and Molecular Dynamics Simulations of Ferrocene–Peptide Conjugates as a Scaffold for Hydrogenase Mimics Lattice Dynamics of a Protein Crystal Lattice dynamics of a protein crystal Lattice dynamics of a protein crystal... Dehydration-driven solvent exposure of hydrophobic surfaces as a driving force in peptide folding... Dehydration-Driven Solvent Exposure of Hydrophobic Surfaces as a Driving Force in Peptide Folding Force-field development and molecular dynamics simulations of ferrocene-peptide conjugates as a scaffold for hydrogenase mimi... Force-field development and molecular dynamics simulations of ferrocene-peptide conjugates as a scaffold for hydrogenase mimi... Realistic Extension Algorithm via Covariance Hessian ... Picosecond Fluctuating Protein Energy Landscape Mapped by Pressure-Temperature Molecular Dynamics Simulation... Molecular dynamics simulations of proteins: can the explicit water model be varied? The structural coupling between ATPase activation and recovery stroke in the myosin II motor... The Structural Coupling between ATPase Activation and Recovery Stroke in the Myosin II Motor The structural coupling between ATPase activation and recovery stroke in the myosin II motor... Transition Networks: A Unifying Theme for Molecular Simulation and Computer Science. Choosing an Appropriate Water Model for Use in Biomolecular Simulations... Molecular Dynamics Simulations of Proteins: Can the Explicit Water Model Be Varied? ... Choosing an Appropriate Water Model for use in Biomolecular Simulations Hierarchical analysis of conformational dynamics in biomolecules: Transition networks of meta-stable states Hierarchical analysis of conformational dynamics in biomolecules: Transition networks of metastable states Molecular dynamics simulations of proteins: can the explicit water model be varied? The principal motions involved in the coupling mechanism of the recovery stroke of the myosin motor. Suppression of the back proton-transfer from Asp85 to the retinal Schiff base in bacteriorhodopsin: A theoretical analysis of structural elements Suppression of the back proton-transfer from Asp85 to the retinal Schiff base in bacteriorhodopsin: A theoretical analysis of structural elements. The principal motions involved in the coupling mechanism of the recovery stroke of the myosin motor. Pagination First page « First Previous page ‹â¶Ä¹ … Page 12 Current page 13 Page 14 … Next page ›â¶Äº Last page Last » Key Links Organizations Biological and Environmental Systems Science Directorate Biosciences Division
