Home Department: Biophysics

Office Address: Theoretical and Computational Biophysics Group
Beckman Institute, Room 3117
University of Illinois at Urbana-Champaign
405 N. Mathews
Urbana, IL 61801

Office Phone: 217-244-1851

Email Address: wenma@ks.uiuc.edu


  • Ph.D. in Biophysics, UIUC, 2016 (expected)

  • B.S. in Physics, Peking University, 2010

Research Interests

I'm interested in understanding structure-function relationships of biomolecules. Specifically I use physical models and simulation tools to link atomistic structures to molecular functions. One important case involves molecular machines, which play vital roles in various processes of living cells. It is a mystery how the chemical energy from ATP is utilized by many molecular machines to fulfill their functions. By combining molecular dynamics simulations with statistical physics, the molecular mechanism and energy landscape of these machines can now be characterized. See our representative publication, as well as our research website here.

Related Research Categories: (publications in parentheses)

  • Mechanism of ring-shaped ATPase motors, such as helicase, unfoldase and F1-ATPase: (1) .
  • Nucleic acid-protein interaction: (1) and (2) .
  • Statistical physics of biomolecules: (1)-SI and (3) .
  • Study of thermodynamics and kinetics of biological processes: (1) and (2) .
  • Publications


    Awards and Honors

    • Graduate College travel grant for Gordon Research Conference - Proteins, 2015
    • Travel award, Biophysical Society 2015 annual meeting
    • Wusi fellowship, Peking University, 2007~2009
    • Freshman scholarship, Peking University, 2006

    Talks and Lectures

    Poster Presentations

    • "Force Generation Mechanism of Molecular Motors." Poster section for NSF site visit to CPLC, University of Illinois, April 2013.
    • "RNA Translocation Coupled to Large-Scale Conformational Transitions of a Hexameric Helicase." 59th Biophysical Society annual meeting, Baltimore, February 2015.
    • "Mechanism of Substrate Translocation by a Ring-Shaped ATPase Motor at Millisecond Resolution." Gordon Research Conference: Proteins, Holderness, June 2015.