Jeremy England, Ph. D
Department of Physics
Jeremy England will join the MIT Physics Department as an Assistant Professor in September 2011. Born in Boston, Jeremy grew up in a small college town near the New Hampshire seacoast. After earning a bachelor's degree in biochemistry from Harvard in 2003, he began his graduate studies at the University of Oxford, and subsequently completed his doctorate in physics at Stanford in 2009. Before coming to MIT, he spent two years as a lecturer and research fellow at Princeton University
Professor England's research is directed towards understanding the patterns of organization in space and time that form the basis of life at the molecular level. Which arrangements of macromolecules in the cytosol are consistent with cell survival? How do a protein's form and function arise from its linear architecture? What are the physical conditions necessary for the emergence of self-replicating molecular forms capable of evolution? What these and other questions of interest all have in common is that they point to theoretical physics as a means to make better sense of fundamentally biological phenomena; the overall objective is to chart a course of inquiry that traces the boundary between inanimate and living matter.
England group aims to span the range from the basically theoretical to the medically practical - theoretical through the construction of analytical models and computer simulations from the concepts of statistical mechanics, and practical through the development of new computational tools for biologists, as well as through the establishment of close collaborations with experimenters in biomedical fields. For example, Prof. England has recently developed a new phenomenological theory of conformational fluctuations in polypeptide chains that successfully predicts the allosteric motions of many globular proteins (Structure, 2011). Future work will not only focus on elaborating this theory's basis in the statistical mechanics of polymers, but also on its use in identifying druggable allosteric sites on proteins, as well as on its application to the in vivo characterization of mutant proteins known to undergo deleterious misfolding and aggregation events that underlie human neurodegenerative disease.
- J. L. England, "Allostery in protein domains reflects a balance of steric and hydrophobic effects." Structure, 2011.
- J. L. England and D. Kaganovich, "Polyglutamine shows a urea-like affinity for unfolded cytosolic protein." FEBS Lett., 2011.
- J. L. England, D. Lucent, and V. S. Pande, "A role for confined water in chaperonin function." J. Am. Chem. Soc., 2008.
- J. L. England and J. Cardy, "Morphogen gradient from a noisy source." Phys. Rev. Lett., 2005.
- J. L. England and E. I. Shakhnovich, "Structural determinant of protein designability." Phys. Rev. Lett., 2003.
Last Updated: July 11, 2011