Structural Dynamics of Free Amino Acids in Diffraction

Authors

  • Dr. I-Ren Lee,

    1. Physical Biology Center for Ultrafast Science and Technology, Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125 (USA)
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  • Dr. Andreas Gahlmann,

    1. Physical Biology Center for Ultrafast Science and Technology, Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125 (USA)
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  • Prof. Ahmed H. Zewail

    Corresponding author
    1. Physical Biology Center for Ultrafast Science and Technology, Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125 (USA)
    • Physical Biology Center for Ultrafast Science and Technology, Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125 (USA)
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  • This work was supported by the National Science Foundation and the Air Force Office of Scientific Research in the Gordon and Betty Moore Center of Physical Biology at Caltech. We thank Dr. Chi-Kung Ni and Dr. Yuri A. Dyakov for their helpful discussions and the sharing of their calculation results.

Abstract

original image

The amino acid tryptophan exhibits complex structural changes both in the ground state, owing to multiple conformations, and upon excitation, because of the involvement of nonradiative pathways. The first report of structural dynamics using combined ultrafast electron diffraction and laser desorption methods is presented.

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