Linked Life Data

7947780

Source:http://linkedlifedata.com/resource/pubmed/id/7947780

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
46
pubmed:dateCreated
1994-12-21
pubmed:abstractText
Surface plasmon resonance (SPR) spectroscopy has been used to follow incorporation and light-induced conformational changes in bovine rhodopsin reconstituted into an egg phosphatidylcholine bilayer deposited on a thin silver film. The magnitude of the SPR spectral changes caused by light varies with pH in a manner paralleling that in flash photolysis experiments, which monitor formation of metarhodopsin II. Irradiation produces an increase of approximately 4 A in the average thickness of the proteolipid layer, consistent with exposure of recognition sites for the G protein. The results demonstrate that the SPR technology described herein may be used to monitor conformational events in membrane-associated receptors such as rhodopsin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13706-11
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Conformational changes in rhodopsin probed by surface plasmon resonance spectroscopy.
pubmed:affiliation
Department of Biochemistry, University of Arizona, Tucson 85721.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't