PHYS 355 |
| Photoactive Yellow Protein (PYP) is responsible for the bacteria Halorhodospira Halophila's ability to respond to the presence of blue light. It is believed that the detected light is absorbed by a chromophore covalently attached to the protein; the resulting photoisomerization of the chromophore initiates a transformation of the protein to its signaling state. However, the time scale of the transformation, (milliseconds) makes the signaling conformation difficult to study by experiment or computation. Recently, Das, Hoff and Clementi used a novel coarse grain model simulation to produce a promising candidate for the signaling state. In this presentation, a plan for gathering some additional evidence on the candidate signaling state is outlined and initial results are presented. Specifically, calculations of the energy differences of the protein and chromophore isomers in key positions of the photocycle will be used to argue for the realism of the candidate signaling state. |
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PHYS Poster Session - Multiscale Modeling in Biophysics
7:30 PM-10:00 PM, Wednesday, April 9, 2008 Morial Convention Center -- Hall A, Poster
Division of Physical Chemistry |