Chemistry and Applications of Retinal Proteins: From Microbes to Humans (#395)
Retinal proteins (rhodopsins) play many important biological roles, ranging from light-driven ion transport to vision, and are found in a wide spectrum of hosts ranging from bacteria to humans. In spite of their diversity, rhodopsins use a common efficient ultrafast photoisomerization of their retinylidene chromophore to store/transfer light energy, ultimately employed to drive the protein function via complex protein-chromophore interactions. While understanding of the atomic-level mechanism of these processes is still actively pursued both experimentally and theoretically, biological and physical chemists are realizing that such an understanding is instrumental for the engineering of novel photoactive materials, including genetically encoded optical probes and light-responsive receptors and actuators. The symposium will cover the latest advances in this field, including: (1) Structural characterization of rhodopsins, e.g., by X-ray crystallography and NMR; (2) Spectroscopic studies of their photochemistry by ultrafast spectroscopy and vibrational techniques; (3) Computational studies of color tuning, light-induced reactions and conformational dynamics; (4) Studies of protein conformational changes by various techniques, including fluorescence, EPR, and NMR; and, finally, the relationship of these fundamental studies with (5) novel applications of retinal proteins as genetically encodable colorimetric and fluorescence probes as well as light-triggered actuators in optogenetics.
Last update: Dec 28, 2015