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Title: Solvation dynamics in protein environments studied by photon echo spectroscopy

Abstract

Photon echo spectroscopy is used to study the mechanisms of solvation dynamics in protein environments at room temperature. Ultrafast and additional multi-exponential long time scales are observed in the three-pulse photon echo peak shift data of the fluorescein dye eosin bound to lysozyme in aqueous solution. The dynamics of the solvated lysozyme are characterized with dielectric continuum models that integrate dielectric data for water with that for lysozyme. By comparing the data with previous results for eosin in water, the authors find that the total coupling of the electronic transition frequency of eosin to the nuclear motions of the aqueous lysozyme solution is smaller than in the aqueous solution. On an ultrafast time scale, solvation appears to be dominated by the surrounding water and not by the ultrafast internal motions of lysozyme. However, over long time scales, lysozyme does contribute significantly, either directly through motions of polar side chains or indirectly through reorientation of the water bound to the surface of the protein.

Authors:
;  [1];  [2];  [3]
  1. Univ. of California, Berkeley, CA (United States). Dept. of Chemistry|[Lawrence Berkeley National Lab., CA (United States). Physical Biosciences Div.
  2. Princeton Univ., NJ (United States)
  3. Iowa State Univ., Ames, IA (United States). Dept. of Chemistry
Publication Date:
Sponsoring Org.:
National Science Foundation, Washington, DC (United States); USDOE, Washington, DC (United States)
OSTI Identifier:
696662
DOE Contract Number:  
FG03-87ER13793
Resource Type:
Journal Article
Journal Name:
Journal of Physical Chemistry B: Materials, Surfaces, Interfaces, amp Biophysical
Additional Journal Information:
Journal Volume: 103; Journal Issue: 37; Other Information: PBD: 16 Sep 1999
Country of Publication:
United States
Language:
English
Subject:
55 BIOLOGY AND MEDICINE, BASIC STUDIES; SOLVATION; DYNAMICS; PROTEINS; EOSIN; LYSOZYME; PHOTONS; SPECTROSCOPY

Citation Formats

Jordanides, X.J., Fleming, G.R., Lang, M.J., and Song, X. Solvation dynamics in protein environments studied by photon echo spectroscopy. United States: N. p., 1999. Web. doi:10.1021/jp9910993.
Jordanides, X.J., Fleming, G.R., Lang, M.J., & Song, X. Solvation dynamics in protein environments studied by photon echo spectroscopy. United States. doi:10.1021/jp9910993.
Jordanides, X.J., Fleming, G.R., Lang, M.J., and Song, X. Thu . "Solvation dynamics in protein environments studied by photon echo spectroscopy". United States. doi:10.1021/jp9910993.
@article{osti_696662,
title = {Solvation dynamics in protein environments studied by photon echo spectroscopy},
author = {Jordanides, X.J. and Fleming, G.R. and Lang, M.J. and Song, X.},
abstractNote = {Photon echo spectroscopy is used to study the mechanisms of solvation dynamics in protein environments at room temperature. Ultrafast and additional multi-exponential long time scales are observed in the three-pulse photon echo peak shift data of the fluorescein dye eosin bound to lysozyme in aqueous solution. The dynamics of the solvated lysozyme are characterized with dielectric continuum models that integrate dielectric data for water with that for lysozyme. By comparing the data with previous results for eosin in water, the authors find that the total coupling of the electronic transition frequency of eosin to the nuclear motions of the aqueous lysozyme solution is smaller than in the aqueous solution. On an ultrafast time scale, solvation appears to be dominated by the surrounding water and not by the ultrafast internal motions of lysozyme. However, over long time scales, lysozyme does contribute significantly, either directly through motions of polar side chains or indirectly through reorientation of the water bound to the surface of the protein.},
doi = {10.1021/jp9910993},
journal = {Journal of Physical Chemistry B: Materials, Surfaces, Interfaces, amp Biophysical},
number = 37,
volume = 103,
place = {United States},
year = {1999},
month = {9}
}