Linked Life Data

7470473

Source:http://linkedlifedata.com/resource/pubmed/id/7470473

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1981-5-13
pubmed:abstractText
Photochemical and fluorescence studies are carried out, exciting bacteriorhodopsin (BR) in its 280-nm absorption band. The data indicate that energy transfer takes place, with a quantum yield of 0.7--0.8, from excited tyrosines and tryptophans to the retinyl chromophore. All of the tyrosine and five to six tryptophan residues are completely quenched by the transfer process while one tryptophan is unquenched and one is partially (approximately 80%) quenched. Energy transfer to the chromophore leads to a photocycle identical with that triggered in (light adapted) bacteriorhodopsin by excitation within the visible absorption bands of the chromophore. The emissive properties of BR in the intact membrane are found equal to those of Triton X-100 solubilized BR monomer. The energy transfer data are discussed in terms of the available amino acid sequence and the electron density map of bacteriorhodopsin. Although such data cannot suggest a single fit between the sequence and the density map (one out of the 7! = 5040 possibilities), they do provide a criterion for testing any specific model for the structure of bacteriorhodopsin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
205-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Photochemistry and fluorescence of bacteriorhodopsin excited in its 280-nm absorption band.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't