John Straub

Professor (Chemistry, MSE)

Professor (Chemistry, MSE)

  • Primary Appointment Chemistry
  • Education NIH Postdoctoral Fellow, Harvard University, 1987-1990 (with Martin Karplus)
    PhD, Columbia University, 1987 (with Bruce Berne)
    MPhil, Columbia University, 1986
    MA, Columbia University, 1984
    BS, University of Maryland, 1982 (with Millard Alexander)
  • Additional Affiliations Materials Science and Engineering
  • Honors and Awards Alfred P. Sloan Research Fellow, 1995-1997
    Metcalf Award for Excellence in Teaching, Boston University, 2005
    Fellow, Institute for Advanced Studies, Hebrew University, Jerusalem, Israel, 1998
    Visiting Professor, Montana State University, Bozeman, Montana, 2006
    JSPS Invitation Fellow, Nagoya University, Nagoya, Japan, 2013
  • Areas of Interest Theoretical and computational chemistry and biophysics.
  • Research Areas The Straub Group investigates fundamental aspects of protein dynamics and thermodynamics underlying the formation of protein structure, through folding and aggregation, and enabling protein function, through pathways of energy flow and signaling. Student and postdoctoral research scientists in the Straub Group work to develop and employ state-of-the-art computational methods while working in collaboration with leading experimental research groups.

    Kinetic and thermodynamic properties defining protein aggregation are elucidated through pioneering computational studies of the earliest stages of amyloid protein aggregation, including the formation of small oligomers (dimers through hexamers) from monomeric protein, and the production of monomeric protein from amyloid precursor proteins.
    Novel computational algorithms for enhanced sampling of conformational ensembles in complex biomolecular systems include effective approaches for global optimization and enhanced conformational sampling, in complex molecular systems, and novel coarse-grained models of proteins, for use in protein structure prediction.
    Novel computational approaches for the exploration of reaction dynamics allow for direct simulation of both ultrafast (quantum) and long-time (classical) dynamical events that translate how protein structure supports dynamical energy flow associated with protein function.
    Pathways and mechanism for energy and signal flow in proteins are explored using classical and quantum dynamical simulations. This includes fundamental aspects of energy transfer associated with ligand binding and redox events in a variety of heme protein systems, with the ultimate goal of relating protein dynamics to function. Professor Straub’s book, “Proteins: Energy, Heat and Signal Flow,” co-edited with David Leitner, captures the state-of-the-art in theoretical studies of protein dynamics and signaling.



Affiliation: Primary & Affiliated Faculty (MSE), Primary Faculty (MSE)