Linked Life Data

17968661

Source:http://linkedlifedata.com/resource/pubmed/id/17968661

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2007-12-28
pubmed:abstractText
The proteorhodopsin family consists of hundreds of homologous retinal containing membrane proteins found in bacteria in the photic zone of the oceans. They are colour tuned to their environment and act as light-driven proton pumps with a potential energetic and regulatory function. Precise structural details are still unknown. Here, the green proteorhodopsin variant has been selected for a chemical shift analysis of retinal and Schiff base by solid-state NMR. Our data show that the chromophore exists in mainly all-trans configuration in the proteorhodopsin ground state. The optical absorption maximum together with retinal and Schiff base chemical shifts indicate a strong interaction network between chromophore and opsin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0925-2738
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15-21
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Characterisation of Schiff base and chromophore in green proteorhodopsin by solid-state NMR.
pubmed:affiliation
Institute for Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J. W. Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't