Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1995-10-12
pubmed:abstractText
The vibrational degrees of freedom of room-temperature rhodopsin (RhRT), the central trans-membrane protein in vision, are measured at room temperature by picosecond resonance coherent anti-Stokes Raman scattering (PR/CARS). High signal-to-noise PR/CARS data for the ethylenic stretching, Schiff base, and hydrogen-out-of-plane modes of the retinal chromophore are quantitatively analyzed via third-order susceptibility relationships. The accurate determination of spectral features permit the PR/CARS bandshapes to be analyzed as a function of RhRT concentration, an essential factor in using picosecond time-resolved CARS techniques to measure the vibrational spectroscopy of picosecond intermediates in the RhRT photosequence. Of particular importance is the recognition that PR/CARS bandshapes are sensitive functions of both the chromophore concentration and the excitation wavelength, as measured relative to the absorption spectra of specific chromophores (static and transient).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:volume
56
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
129-35
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Vibrational spectra of room-temperature rhodopsin: concentration dependence in picosecond resonance coherent anti-Stokes Raman scattering.
pubmed:affiliation
Department of Chemistry, University of Arizona, Tucson 85721, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't