Linked Life Data

17445804

Source:http://linkedlifedata.com/resource/pubmed/id/17445804

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2007-5-7
pubmed:abstractText
Structural characterization of membrane proteins is hampered by the instability of the isolated proteins in detergent solutions. Here, we describe a new class of phospholipid-like surfactants that stabilize the G protein-coupled receptor, BLT1. These compounds, called C(13)U(9), C(13)U(19), C(15)U(25) and C(17)U(16), were synthesized by radical polymerization of Tris(hydroxymethyl) acrylamidomethane in the presence of thioglycerol, first endowed with two hydrocarbon chains with variable lengths (13-17 carbon atoms), as transfer reagent. C(13)U(19), C(17)U(16) or C(15)U(25) significantly enhanced the stability of BLT1 in solution compared to what was obtained with common detergents. These molecules therefore represent a promising step towards the structural characterization of BLT1 and possibly other membrane proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
581
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1944-50
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
New tensio-active molecules stabilize a human G protein-coupled receptor in solution.
pubmed:affiliation
Institut des Biomolécules Max Mousseron, UMR 5247 CNRS-Universités Montpellier I et II, Faculté de Pharmacie, 15 Av. Ch. Flahault, BP 14491, 34093 Montpellier Cedex 5, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't