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Mapping GFP structure evolution during proton transfer with femtosecond Raman spectroscopy

Author

Listed:
  • Chong Fang

    (University of California, Berkeley, California 94720, USA)

  • Renee R. Frontiera

    (University of California, Berkeley, California 94720, USA)

  • Rosalie Tran

    (University of California, Berkeley, California 94720, USA)

  • Richard A. Mathies

    (University of California, Berkeley, California 94720, USA)

Abstract

Inside green fluorescent protein GFP, the green fluorescent protein from the jellyfish Aequorea victoria, is widely used in the life sciences as a gene expression marker because of its efficient bioluminescence. The atomistic details of the excited-state proton transfer that generates this bioluminescence are still not fully understood. Fang et al. have used femtosecond stimulated Raman spectroscopy of the GFP chromophore to obtain detailed time-resolved vibrational spectra that reveal how a low-frequency skeletal vibration poises the protein for the critical proton transfer process. As well as throwing light on a reaction central to countless biological studies, this method of making real-time observations of the structural changes of a molecule during a multidimensional chemical reaction should have broad application in the determination of reaction mechanisms.

Suggested Citation

  • Chong Fang & Renee R. Frontiera & Rosalie Tran & Richard A. Mathies, 2009. "Mapping GFP structure evolution during proton transfer with femtosecond Raman spectroscopy," Nature, Nature, vol. 462(7270), pages 200-204, November.
    • Handle: RePEc:nat:nature:v:462:y:2009:i:7270:d:10.1038_nature08527
    DOI: 10.1038/nature08527
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    Cited by:

    1. Takahisa Suzuki & Seisuke Arai & Mayumi Takeuchi & Chiye Sakurai & Hideaki Ebana & Tsunehito Higashi & Hitoshi Hashimoto & Kiyotaka Hatsuzawa & Ikuo Wada, 2012. "Development of Cysteine-Free Fluorescent Proteins for the Oxidative Environment," PLOS ONE, Public Library of Science, vol. 7(5), pages 1-16, May.

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