What I do
My work aims to build mathematical models based on principles of physics and chemistry to seek fundamental principles in biology. These models -- in combination with computer simulations and collaboration with experimental colleagues -- allow us to address diverse range of problems in molecular and cellular biophysics, such as: 1) Can we understand the origin of extreme thermal tolerance of heat loving organisms in terms of their constituent protein molecules? 2) Likewise, what can we say about proteins in the ancient organisms that cease to exist today but are believed to have lived in hot environment at the beginning of the life? 3) What can we learn about molecular wizardry inside cells by carefully looking at the sense-less fluctuations typically measured in many biological experiments (involving cells) but thrown away as nuisance? We claim the "truth is in the noise".
When I teach, my goal is to generate passion among students to discover the heart of the problem. I intend to drive home a big-picture appreciation for the fundamental principles of physics. Starting from these principles, we subsequently build application problems and derive concepts. While I typically teach traditional physics courses, I also like to showcase the power of numeracy skills, consistency checks to question hypothesis and build models to answer many other complex problems that reside outside the realm of traditional physics classes.
During my PHD at the University of Massachusetts, Amherst I learned to use Statistical Physics principles to problems in Polymer Science.
After my PHD, I worked in the University of California, San Francisco as a Post Doctoral Scholar to further my interest in Biological problems.
In 2008 I joined University of Denver as an Assistant Professor.
- MS, Physics, University of Massachusetts, 2003
- Ph.D., University of Massachusetts, 2003
- MS, Physics, Indian Institute of Technology, 1997
- American Physics Society
- Protein Folding Consortium sponsored by National Science Foundation
We are interested in applying these proteins models to build a quantitative framework for the proteome (collection of all the proteins insides a cell).
In a separate direction we develop models of stochastic biological processes using the principle of Maximum Caliber. We are applying this principle in diverse biological problems: modeling gene networks, to cell shape changes in cancer cells.
- CAREER:How Do Thermophillic Proteins Withstand High Temperature?
- Modulating charge patterning and ionic strength as a strategy to induce conformational changes in intrinsically disordered proteins
- Sequence charge decoration dictates coil-globule transition in Intrinsically Disordered Proteins
- A theoretical method to compute sequence dependent configurational properties in charged polymers and proteins
- All-atom simulations reveal protein charge decoration in the folded and unfolded ensemble is key in thermophilic adaptation
- Ancient Thioredoxins evolved to modern day Stability-Function requirement by altering Native State ensemble
- Using polymer physics to investigate the folded and unfolded proteome
- Truth is in the Disorder
- PROTEOME FOLDING, FEYNMAN DIAGRAM AND EVOLUTION
- Truth is in the Disorder and Noise
- Principle of Maximum Caliber: a variational approach to model stochastic dynamics
- NSF CAREER AWARD, National Science Foundation
- Cottrell Scholar Award, Research Corporation for Science Advancement
- Selected as a Scialog Fellow, Research Corporation for Science Advancement and the Gordon and Betty Moore Foundation