Devarajan Thirumalai

Distinguished University Professor


  • B. S. Indian Institute of Technology Kanpur 1977
  • Ph. D. University of Minnesota, 1982, (Advisor: Prof D. G. Truhlar)
  • Post Doctoral Fellow, Columbia University 1982-1985 (Advisor: Prof. B. J. Berne)

 Professional Experience

  •  Director, Biophysics Program University of Maryland (2005 – present);
  • Editorial Board J. Chemical Physics (2008-present);
  • Editorial Board Protein Evolution, Design, and Selection (2005-present).
  • Served in the Editorial boards of Theoretical Chemistry Accounts, Communication in Mathematical Methods.

 Research Interests

Research in Dr. Thirumalai’s group focuses on various problems in equilibrium and non equilibrium statistical mechanics. Currently various aspects of the transition from liquid to amorphous state are being investigated. Another area of research involves the theoretical study of polymer-colloid interactions. Research is also being carried out to understand the dynamics of protein folding.

 Maryland Biophysics Program

Professional Societies

Biophysical Society

Major Recognitions and Honors

  • National Science Talent Research Fellow, India 1972-1977
  • Camille and Henry Dreyfus Foundation 1985-1987
  • Distinguished New Faculty Award
  • Alfred P. Sloan Fellowship 1986-1988
  • Presidential Young Investigator Award 1987-1992
  • Outstanding Junior Faculty Award 1989
  • Camille and Henry Dreyfus Foundation 1990
  • Maryland Outstanding Young Scientist 1995
  • Distinguished Faculty Research Fellowship Award 1998

 Students Mentored

Over 30 students and postdoctoral fellows have trained with me. The majority of them are in academic positions.

Theoretical chemistry and Biophysics

The major focus of research in our group is to develop quantitative theoretical and computational methods to solve major problems in biology. We tackle a broad range of problems in biophysics using principles of statistical mechanics, polymer physics, and many computational techniques. Summaries of some of the areas that we are working on are given below.

Function of molecular chaperones: Although most proteins fold spontaneously in order to carry out their functions a few misfold, and can potentially aggregate. To guard against this aberrant phenomenon nature has evolved molecular chaperones that can recognize and rescue the misfolded structures. The most intensely studied chaperone is GroEL, which undergoes complex structural transformations in response to ATP binding. Together with Prof. George H. Lorimer we are working to provide a molecular basis for the function of this ATP-driven machine.

Single Molecule Force Spectroscopy: The ultimate dram of watching proteins and RNA fold one molecule at a time is starting to be realized with
advances in single molecule methods. In order to fully realize the scope these advances it is important to develop theoretical methods that can uncover the folding landscape of biomolecules using experimental input. We are developing some of the most advanced methods that provide mechanism of how proteins, RNA, and protein complexes respond to mechanical force.

Protein aggregation and link to diseases: It is now firmly established that a number of diseases (Alzheimer’s, Parkinson’s, mad cow disease etc) are linked to aggregation of specific proteins. The mechanisms of aggregation and their structures are largely unknown. We are using Molecular Dynamics
simulations to provide microscopic details of how low order aggregates form. The biophysical results provide clues in devising drugs that can prevent aggregation in proteins.

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