Advanced

Does the Dynamic Stokes Shift Report on Slow Protein Hydration Dynamics?

Halle, Bertil LU and Nilsson, Lennart (2009) In The Journal of Physical Chemistry Part B 113(24). p.8210-8213
Abstract
The time-dependent fluorescence frequency shift of protein-attached probes has a much slower decay than that for the free probe. The decay times, ranging from 10 ps to several nanoseconds, have been attributed to hydration water motions several orders of magnitude slower than those in the hydration shell of small solutes. This interpretation deviates strongly from the prevailing picture of protein hydration dynamics. We argue here that the slow decay in the fluorescence shift can be explained by a ubiquitous solvent polarization mechanism, with no need to invoke slow water motions or a dynamic coupling with protein motions. This mechanism can be qualitatively understood with the aid of a dielectric continuum model. We therefore conclude... (More)
The time-dependent fluorescence frequency shift of protein-attached probes has a much slower decay than that for the free probe. The decay times, ranging from 10 ps to several nanoseconds, have been attributed to hydration water motions several orders of magnitude slower than those in the hydration shell of small solutes. This interpretation deviates strongly from the prevailing picture of protein hydration dynamics. We argue here that the slow decay in the fluorescence shift can be explained by a ubiquitous solvent polarization mechanism, with no need to invoke slow water motions or a dynamic coupling with protein motions. This mechanism can be qualitatively understood with the aid of a dielectric continuum model. We therefore conclude that the long decay times measured with time-dependent fluorescence spectroscopy contain no information about protein hydration dynamics. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry Part B
volume
113
issue
24
pages
8210 - 8213
publisher
The American Chemical Society
external identifiers
  • wos:000266930200003
  • pmid:19462949
  • scopus:67149126766
ISSN
1520-5207
DOI
10.1021/jp9027589
language
English
LU publication?
yes
id
8068084f-f6d3-4c8e-a2c6-97bee5402537 (old id 1412076)
date added to LUP
2009-06-11 08:47:53
date last changed
2017-12-10 04:05:12
@article{8068084f-f6d3-4c8e-a2c6-97bee5402537,
  abstract     = {The time-dependent fluorescence frequency shift of protein-attached probes has a much slower decay than that for the free probe. The decay times, ranging from 10 ps to several nanoseconds, have been attributed to hydration water motions several orders of magnitude slower than those in the hydration shell of small solutes. This interpretation deviates strongly from the prevailing picture of protein hydration dynamics. We argue here that the slow decay in the fluorescence shift can be explained by a ubiquitous solvent polarization mechanism, with no need to invoke slow water motions or a dynamic coupling with protein motions. This mechanism can be qualitatively understood with the aid of a dielectric continuum model. We therefore conclude that the long decay times measured with time-dependent fluorescence spectroscopy contain no information about protein hydration dynamics.},
  author       = {Halle, Bertil and Nilsson, Lennart},
  issn         = {1520-5207},
  language     = {eng},
  number       = {24},
  pages        = {8210--8213},
  publisher    = {The American Chemical Society},
  series       = {The Journal of Physical Chemistry Part B},
  title        = {Does the Dynamic Stokes Shift Report on Slow Protein Hydration Dynamics?},
  url          = {http://dx.doi.org/10.1021/jp9027589},
  volume       = {113},
  year         = {2009},
}