Linked Life Data

19462949

Source:http://linkedlifedata.com/resource/pubmed/id/19462949

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2009-6-11
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1520-6106
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
113
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8210-3
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Does the dynamic Stokes shift report on slow protein hydration dynamics?
pubmed:affiliation
Biophysical Chemistry, Center for Molecular Protein Science, Lund University, SE-22100 Lund, Sweden. bertil.halle@bpc.lu.se
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't