dc.creator Yang, J. en_US dc.creator Zhang, L. en_US dc.creator Wang, L. en_US dc.creator Zhong, D. en_US dc.date.accessioned 2013-07-16T21:46:35Z dc.date.available 2013-07-16T21:46:35Z dc.date.issued 2013 en_US dc.identifier 2013-FE-08 en_US dc.identifier.uri http://hdl.handle.net/1811/55569 dc.description Author Institution: Department of Physics, The Ohio State University, Columbus, OH 43210; Department of Chemistry, Columbia University, New York, NY 10027; Department of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics, and Biochemistry, The Ohio State University, Columbus, OH 43210 en_US dc.description.abstract Water motion probed by intrinsic tryptophan shows the significant slowdown around protein surfaces but it is unknown how the ultrafast internal conversion of two nearly degenerate states of Trp ($^1$L$_a$ and $^1$L$_b$) affects the initial hydration in proteins. Here, we used a mini-protein with ten different tryptophan locations one at a time through site-directed mutagenesis and extensively characterized the conversion dynamics of the two states. We observed all the conversion time scales in 40-80 fs by measurement of their anisotropy dynamics. This result is significant and shows no noticeable effect on the initial observed hydration dynamics and unambiguously validates the slowdown of hydration layer dynamics as shown here again in two mutant proteins. en_US dc.language.iso en en_US dc.publisher Ohio State University en_US dc.title FEMTOSECOND CONICAL INTERSECTION DYNAMICS OF TRYPTOPHAN IN PROTEINS AND VALIDATION OF SLOWDOWN OF HYDRATION LAYER DYNAMICS en_US dc.type Article en_US dc.type Image en_US dc.type Presentation en_US
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