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Peptide deactivation

Spectroscopy meets theory

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Combined spectroscopic measurements and theoretical calculations bring to light an ultrafast excited-state deactivation process in peptides that may contribute to the ultraviolet photostability of proteins.

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Figure 1: The three most stable and experimentally detected conformers of NAPA.
Figure 2: Schematic potential-energy profiles of the electronic ground state (S0, black), the lowest locally excited state (LE, blue) and charge-transfer state (CT, red) of the B conformer of NAPA along the minimum-energy path for proton transfer.

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Authors and Affiliations

  1. Wolfgang Domcke is in the Department of Chemistry, Technische Universität München, D-85747 Garching, Germany,

    Wolfgang Domcke

  2. Andrzej L. Sobolewski is in the Institute of Physics, Polish Academy of Sciences, PL-02668 Warsaw, Poland,

    Andrzej L. Sobolewski

Authors
  1. Wolfgang Domcke
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  2. Andrzej L. Sobolewski
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Correspondence to Wolfgang Domcke or Andrzej L. Sobolewski.

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Domcke, W., Sobolewski, A. Spectroscopy meets theory. Nature Chem 5, 257–258 (2013). https://doi.org/10.1038/nchem.1601

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