Haw Yang, Associate Professor
Department of Chemistry
Insights from Single-Molecule Protein Dynamics—Conformation Bias, Local Unfolding, and Architectural Encoding
On one hand, the three-dimensional organization of a protein can now be quickly and routinely determined with atomistic precision. On the other hand, previously unknown protein functions continue to be identified and exploited at an ever increasing speed, as well new chemical-biology tools are being invented at a breathtaking pace, providing unprecedented new ways to study and engineer proteins. Yet, weaving through these exciting developments at both ends of protein science (structure and function) is a piece of basic science in biophysics that would prove to be a fertile land for the creative—the prediction of the functionally relevant dynamics of a protein given a snapshot of its structure. A major impediment to achieving this goal is the lack of information detailing the manner by which a protein reorganizes its structure in under the sway of thermal fluctuations. In this context, one may argue that time-dependent single-molecule spectroscopy is the experimental means to afford a direct access to real-time molecular dynamics, and that molecular dynamics (MD) simulation the computation-theoretical tool to offer atomistic insights. This presentation will cover some examples that highlight the developments of high-precision single-molecule experiments and the integration with high-level computations, discuss the conceptual advances they enable in protein biophysics, and speculate on the future prospects of bridging the MD and experimental time scales.
|Time : Tuesday, November 19, 2013, 01:00pm - 02:00pm|
|Location : Laufer Center Lecture Hall 101|
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