U.S. Department of Health and Human Services
Robert Best

 Contact Info

Tel: 301-496-5414
Email: robert.best2@nih.gov

 Select Experience

  • United Kingdom Royal Society University Research FellowUniversity of Cambridge2007–2012
  • Ph.D.University of Cambridge2003

 Related Links


Robert B. Best, Ph.D.

Senior Investigator, Theoretical Biophysical Chemistry SectionLaboratory of Chemical Physics
  • Biomedical Engineering/ Biophysics/ Physics, Computational Biology/ Bioinformatics/ Biostatistics/ Mathematics, Structural Biology
Research Summary/In Plain Language

Research in Plain Language

I use computational methods to study the function of large biological molecules. For example, we are interested in learning how proteins “fold” to their native structures.  Protein folding is the process by which a polypeptide chain, initially in a highly disordered state, self-assembles into a unique 3-dimensional native structure.  Since the native structure is usually required for the protein to function, it is important to understand how this structure is assembled.  In addition, many diseases are caused by protein misfolding, in which proteins form structures other than the native one, often by sticking to each other.  Therefore, it is also important to know how such misfolding occurs and what structures are formed.

In collaboration with experimental groups, we use computational and theoretical methods to obtain new insights into protein folding and misfolding.  In particular, we are interested in single molecule experiments, which we can use to resolve sub-populations of folded and misfolded states, rather than producing an average over a very large number of molecules.