Linked Life Data

7492549

Source:http://linkedlifedata.com/resource/pubmed/id/7492549

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
47
pubmed:dateCreated
1996-1-11
pubmed:abstractText
The role of Trp and Tyr residues in determining membrane protein structure is particularly interesting because indole and phenol structures combine hydrophobic and polar groups, and it is hard to predict the exact region of the membrane at which their energy would be at a minimum. To determine the depths intrinsically favored by these residues, the locations of membrane-associating Trp and Tyr analogs have been determined using a fluorescence quenching technique able to measure depth at high resolution. They are found to locate at the same depths as Trp and Tyr in membrane proteins, 14-15 A from the bilayer center, which implies an important role for these residues in aligning membrane proteins in precise relationship to the lipid bilayer.
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
28
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15475-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Anchoring of tryptophan and tyrosine analogs at the hydrocarbon-polar boundary in model membrane vesicles: parallax analysis of fluorescence quenching induced by nitroxide-labeled phospholipids.
pubmed:affiliation
Department of Biochemistry and Cell Biology, State University of New York at Stony Brook 11794-5215, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.