Campus Units

Chemistry

Document Type

Article

Publication Version

Published Version

Publication Date

9-1999

Journal or Book Title

Journal of Physical Chemistry B

Volume

103

Issue

37

First Page

7995

Last Page

8005

DOI

10.1021/jp9910993

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 our data with previous results for eosin in water [Lang, M. J.; Jordanides, X. J.; Song, X.; Fleming, G. R. J. Chem. Phys. 1999, 110, 5584], we 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.

Comments

Reprinted (adapted) with permission from Journal of Physical Chemistry B 103 (1999): 7995, doi:10.1021/jp9910993. Copyright 1999 American Chemical Society.

Copyright Owner

American Chemical Society

Language

en

File Format

application/pdf

Included in

Chemistry Commons

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