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Ultrafast energy relaxation dynamics of amide I vibrations coupled with protein-bound water molecules

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  • Junjun Tan

    (University of Science and Technology of China)

  • Jiahui Zhang

    (University of Science and Technology of China)

  • Chuanzhao Li

    (University of Science and Technology of China)

  • Yi Luo

    (University of Science and Technology of China)

  • Shuji Ye

    (University of Science and Technology of China)

Abstract

The influence of hydration water on the vibrational energy relaxation in a protein holds the key to understand ultrafast protein dynamics, but its detection is a major challenge. Here, we report measurements on the ultrafast vibrational dynamics of amide I vibrations of proteins at the lipid membrane/H2O interface using femtosecond time-resolved sum frequency generation vibrational spectroscopy. We find that the relaxation time of the amide I mode shows a very strong dependence on the H2O exposure, but not on the D2O exposure. This observation indicates that the exposure of amide I bond to H2O opens up a resonant relaxation channel and facilitates direct resonant vibrational energy transfer from the amide I mode to the H2O bending mode. The protein backbone motions can thus be energetically coupled with protein-bound water molecules. Our findings highlight the influence of H2O on the ultrafast structure dynamics of proteins.

Suggested Citation

  • Junjun Tan & Jiahui Zhang & Chuanzhao Li & Yi Luo & Shuji Ye, 2019. "Ultrafast energy relaxation dynamics of amide I vibrations coupled with protein-bound water molecules," Nature Communications, Nature, vol. 10(1), pages 1-6, December.
  • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08899-3
    DOI: 10.1038/s41467-019-08899-3
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    Cited by:

    1. Yuening Zhang & Xujin Qin & Xuefeng Zhu & Minghua Liu & Yuan Guo & Zhen Zhang, 2022. "Direct observation of long-range chirality transfer in a self-assembled supramolecular monolayer at interface in situ," Nature Communications, Nature, vol. 13(1), pages 1-9, December.

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