4.8 Article

Ultrafast Dynamics of Protein Proton Transfer on Short Hydrogen Bond Potential Energy Surfaces: S65T/H148D GFP.

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 5, Pages 1452-+

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/ja907690g

Keywords

-

Funding

  1. EPSRC
  2. NSF [CHE-0822587]
  3. U.S. Public Health Services [DK-007521]
  4. EPSRC [EP/E010466/1] Funding Source: UKRI
  5. Division Of Chemistry
  6. Direct For Mathematical & Physical Scien [822587] Funding Source: National Science Foundation

Ask authors/readers for more resources

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

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.8
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available