Linked Life Data

19854176

Source:http://linkedlifedata.com/resource/pubmed/id/19854176

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
2009-11-17
pubmed:abstractText
Channelrhodopsin-2 mediates phototaxis in green algae by acting as a light-gated cation channel. As a result of this property, it is used as a novel optogenetic tool in neurophysiological applications. Structural information is still scant and we present here the first resonance Raman spectra of channelrhodopsin-2. Spectra of detergent solubilized and lipid-reconstituted protein were recorded under pre-resonant conditions to exclusively probe retinal in its electronic ground state. All-trans retinal was identified to be the favoured configuration of the chromophore but significant contributions of 13-cis were detected. Pre-illumination hardly changed the isomeric composition but small amounts of presumably 9-cis retinal were found in the light-adapted state. Spectral analysis suggested that the Schiff base proton is strongly hydrogen-bonded to a nearby water molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1873-3468
pubmed:author
pubmed:issnType
Electronic
pubmed:day
19
pubmed:volume
583
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3676-80
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
The retinal structure of channelrhodopsin-2 assessed by resonance Raman spectroscopy.
pubmed:affiliation
Bielefeld University, Biophysical Chemistry, 33615 Bielefeld, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't