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Ultrafast dynamics of protein proton transfer on short hydrogen bond potential energy surfaces: S65T/H148D GFP.
J Am Chem Soc. 2010 Feb 10; 132(5):1452-3.JA

Abstract

Ultrafast proton transfer dynamics on a short H-bond in a protein were studied through the time-resolved fluorescence of the S65T/H148D green fluorescent protein (GFP) mutant. In response to the change in chromophore pK(a) upon excitation, the donor-proton-acceptor structure evolves on a sub-100 fs time scale, followed by picosecond time scale vibrational cooling and host structure reorganization.

Authors+Show Affiliations

School of Chemistry, University of East Anglia, Norwich NR4 7TJ, UK.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

19916498

Citation

Kondo, Minako, et al. "Ultrafast Dynamics of Protein Proton Transfer On Short Hydrogen Bond Potential Energy Surfaces: S65T/H148D GFP." Journal of the American Chemical Society, vol. 132, no. 5, 2010, pp. 1452-3.
Kondo M, Heisler IA, Stoner-Ma D, et al. Ultrafast dynamics of protein proton transfer on short hydrogen bond potential energy surfaces: S65T/H148D GFP. J Am Chem Soc. 2010;132(5):1452-3.
Kondo, M., Heisler, I. A., Stoner-Ma, D., Tonge, P. J., & Meech, S. R. (2010). Ultrafast dynamics of protein proton transfer on short hydrogen bond potential energy surfaces: S65T/H148D GFP. Journal of the American Chemical Society, 132(5), 1452-3. https://doi.org/10.1021/ja907690g
Kondo M, et al. Ultrafast Dynamics of Protein Proton Transfer On Short Hydrogen Bond Potential Energy Surfaces: S65T/H148D GFP. J Am Chem Soc. 2010 Feb 10;132(5):1452-3. PubMed PMID: 19916498.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Ultrafast dynamics of protein proton transfer on short hydrogen bond potential energy surfaces: S65T/H148D GFP. AU - Kondo,Minako, AU - Heisler,Ismael A, AU - Stoner-Ma,Deborah, AU - Tonge,Peter J, AU - Meech,Stephen R, PY - 2009/11/18/entrez PY - 2009/11/18/pubmed PY - 2010/3/13/medline SP - 1452 EP - 3 JF - Journal of the American Chemical Society JO - J. Am. Chem. Soc. VL - 132 IS - 5 N2 - Ultrafast proton transfer dynamics on a short H-bond in a protein were studied through the time-resolved fluorescence of the S65T/H148D green fluorescent protein (GFP) mutant. In response to the change in chromophore pK(a) upon excitation, the donor-proton-acceptor structure evolves on a sub-100 fs time scale, followed by picosecond time scale vibrational cooling and host structure reorganization. SN - 1520-5126 UR - https://www.unboundmedicine.com/medline/citation/19916498/Ultrafast_dynamics_of_protein_proton_transfer_on_short_hydrogen_bond_potential_energy_surfaces:_S65T/H148D_GFP_ L2 - https://dx.doi.org/10.1021/ja907690g DB - PRIME DP - Unbound Medicine ER -