Robert B. Best, Ph.D.
Theoretical Biophysical Chemistry Section, Laboratory of Chemical Physics
Building 5, Room 130
5 Memorial Drive
Bethesda, MD 20814
My research is concerned with the dynamics of large biomolecules and in particular with protein dynamics, folding, and misfolding. Novel simulation and theoretical methods are developed as needed to address specific problems. A strong emphasis is placed on making a connection with experiment, both in using experimental data to help improve simulation methodology or sampling, and simulations as a tool to assist the interpretation of results.
Recent work has focused on the following:
- the optimization of protein force fields using empirical data for peptides and macromolecules in solution;
- interpretation of single-molecule fluorescence or pulling experiments using simulation and theory;
- coarse-grained master equations as a tool for interpreting peptide dynamics in simulations;
- diffusion models of protein folding;
- the binding mechanism of intrinsically disordered proteins;
- the influence of molecular chaperonins on folding and misfolding;
- the mechanism of substrate transport in hydrogenase enzymes; and
- methods for identifying cryptic binding pockets in proteins.
To view more about my research, visit my lab's website.
- United Kingdom Royal Society University Research Fellow, University of Cambridge, 2007–2012
- Ph.D., University of Cambridge, 2003
Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. Extreme disorder in an ultrahigh-affinity protein complex. Nature. 2018;555(7694):61-66.
Tian P, Louis JM, Baber JL, Aniana A, Best RB. Co-Evolutionary Fitness Landscapes for Sequence Design. Angew Chem Int Ed Engl. 2018;57(20):5674-5678.
Domański J, Sansom MSP, Stansfeld PJ, Best RB. Balancing Force Field Protein-Lipid Interactions To Capture Transmembrane Helix-Helix Association. J Chem Theory Comput. 2018;14(3):1706-1715.
Zerze GH, Mittal J, Best RB. Diffusive Dynamics of Contact Formation in Disordered Polypeptides. Phys Rev Lett. 2016;116(6):068102.
Best RB, Hummer G. Microscopic interpretation of folding ϕ-values using the transition path ensemble. Proc Natl Acad Sci U S A. 2016;113(12):3263-8.
Related Scientific Focus Areas
Biomedical Engineering and Biophysics
This page was last updated on January 31st, 2016