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With the burgeoning of research into the proteome over the past decade, our knowledge of the structure and function of individual proteins has become increasingly exhaustive. Markedly less exhaustive is our knowledge of how proteins function as they do in vivo -- in the presence of a profusion of other biomolecules at high concentrations. In such dense environments, folding and complexation become highly frustrated, leading proteins to explore regions of their conformation space not expected on the basis of their crystal structures alone, thereby fundamentally altering their anticipated function.
Past work using Go-like lattice models has illustrated that in environments crowded by polymers or other proteins, folding is influenced just as strongly by entropy as by potential energy. Excluded volume effects can bias proteins toward folding and complexation along alternative pathways, or preclude folding and complexation altogether. In the future, I hope to extend these seminal efforts toward even more crowded membrane protein environments, where both experimental and computational techniques have, to date, fallen short. Of key interest is determining the precise physical role of membrane lipids in stabilizing membrane self-assembly processes in the absence of ligands. Equally crucial is the development of new physical and computational methods to facilitate further research. In such cramped environments, Monte Carlo techniques largely fail, necessitating the evolution of more advanced statistical and computational approaches.
Another recurring theme of my research is the ultrafast dynamics of liquids and glasses. Recent theoretical work in this arena has inspired new spectroscopic techniques for observing axially-symmetric liquid crystal systems, while future work will focus upon developing formalism to better understand glassy dynamics.
Rubenstein, B. and L. Kaufman. The Role of Extracellular Matrix in Glioma Invasion: A Cellular Potts Model Approach. Biophysical Journal. 95: 5661-5680, 2008.
Rubenstein, B., Coluzza, I., and M.A. Miller. An Entropic Binding Fitness?: Protein Binding Amid Polymer Brushes. In preparation. To be submitted to Nanoletters in January 2009.
Rubenstein, B., Coluzza, I., and M.A. Miller. Protein Folding and Binding in Dense Environs. In preparation. To be submitted to Biophysical Journal in January 2009.
Rubenstein, B. Protein Folding and Binding Amidst Entropy Sources. M. Phil. Thesis. University of Cambridge, August 2008.
Rubenstein, B. and R. Stratt. Highlighting Liquid Crystal Dynamics and Phase Transitions via Polarization Selectivity. In (further) preparation. Expected Submission to the Journal of Physical Chemistry B, February 2009.
Rubenstein, B., Gubernatis, J.G., and J.D. Doll. Comparative Monte Carlo Efficiency by Monte Carlo Analysis. Expected Submission to Physical Review B, 2010. arXiv:1004.0931v1.
Conferences
Rubenstein, B. A Stochastic Approach to Glioblastoma Invasion Amidst Collagen I.
American Chemical Society Meeting in Chicago Physical Chemistry Undergraduate Poster Session, April, 2007.
Rubenstein, B. Protein Folding and Self-Assembly Amidst Entropy Sources. Fall 2008 American Chemical Society Meeting in Philadelphia Physical Chemistry General Poster Session, August 2008.
Rubenstein, B. Should One Just Accept the Acceptance Ratio? Los Alamos National Laboratory Student Symposium, Physics Division, August 2009.
Rubenstein, B.M. Comparative Monte Carlo Efficiency by Monte Carlo Analysis, NY Theoretical and Computational Chemistry Conference, CUNY Graduate Center, NY, NY, January 11, 2010.
Rubenstein, B.M. Exact Ground State Properties of Nearly Infinite Strongly Correlated Electron Systems via the Monte Carlo Power Method. SIAM PP10, Seattle, Washington, Feb. 23-27, 2010.
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