Linked Life Data

20085749

Source:http://linkedlifedata.com/resource/pubmed/id/20085749

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2010-3-15
pubmed:abstractText
SNARE proteins are implicated in membrane fusion during neurotransmission and peptide hormone secretion. Relatively little is known about the molecular interactions of their trans- and juxtamembrane domains with lipid membranes. Here, we report the structure and the assembling behavior of one of the SNARE proteins, VAMP1/synaptobrevin1 incorporated in a lipid monolayer at an air-water interface which mimics the membrane environment. Our results show that the protein is extremely sensitive to surface pressure as well as the lipid composition. Monolayers of proteins alone or in the presence of the neutral phospholipid DMPC underwent structural transition from alpha-helix to beta-sheet upon surface compression. In contrast, the anionic phospholipid DMPG inhibited this transition in a concentration-dependent manner. Moreover, the orientation of the proteins was highly sensitive to the charge density of the lipid layers. Thus, the structure of VAMP1 is clearly controlled by protein-lipid interactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:copyrightInfo
2010 Elsevier B.V. All rights reserved.
pubmed:issnType
Print
pubmed:volume
1798
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
928-37
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Effect of monolayer lipid charges on the structure and orientation of protein VAMP1 at the air-water interface.
pubmed:affiliation
Université de Bordeaux, UMR CBMN 5248, CNRS, Institut Européen de Chimie et Biologie, 2 Rue Robert Escarpit, F-33607 PESSAC, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't