Linked Life Data

6854643

Source:http://linkedlifedata.com/resource/pubmed/id/6854643

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-7-29
pubmed:abstractText
We have used vesicles made from delipidated bacteriorhodopsin and synthetic lecithins to address the following questions. If the transmembrane dimension of a protein hydrophobic surface differs from the equilibrium thickness of its lipid bilayer environment, will protein monomers aggregate to decrease the protein-lipid contact surface area? If so, how large must the difference be to induce aggregation? Using lecithins with acyl chains from di-10:0 to di-24:1, the thickness of the bilayer hydrocarbon region above the lipid phase transition temperature (tm) was varied from 14.5 A less than to 7.5 A more than the transmembrane dimension of the bacteriorhodopsin hydrophobic region. Bacteriorhodopsin remains dispersed when the surrounding bilayer hydrophobic region is 4 A thicker or 10 A thinner than the bacteriorhodopsin hydrophobic surface. Only the thin- (10:0) and thick- (24:1) bilayer samples showed any bacteriorhodopsin aggregation above tm. Thus a surprisingly large difference between protein and lipid hydrophobic thicknesses can be accommodated without protein aggregation. The lipid bilayer can evidently sustain large local distortions with a small change in free energy.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
166
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
203-10
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Bacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thicknesses.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.