Linked Life Data

8373787

Source:http://linkedlifedata.com/resource/pubmed/id/8373787

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-10-21
pubmed:abstractText
The interaction of myelin basic protein (MBP) with single bilayers on a solid support (planar and spherical support) is studied by deuterium nuclear magnetic resonance (2H-NMR), differential scanning calorimetry (DSC) and polarized attenuated total reflection infrared spectroscopy (ATR-IR). The single bilayer consisted of either DMPC or of a binary mixture of DMPC with 10-20 mol% of an acidic phospholipid (DMPG, DMPS or DMPA). All methods applied indicate that MBP strongly interacts with the binary lipid systems but not with the pure DMPC bilayers. The interaction is predominantly electrostatic in nature and does not depend on the choice of a particular acidic lipid (for the binary systems). In particular, the results give no indication for a hydrophobic interaction of MBP with the membrane. Our data provide evidence that, in contrast to previous findings, no demixing and/or domain formation in the binary systems is induced due to the MBP coupling. The infrared order parameter was determined for both lipid components of the binary systems and shows a remarkable change for both lipids due to the interaction with MBP while the NMR order parameter remained essentially unchanged. This is discussed in terms of the different timescales characteristic for both methods. The single supported bilayer responds to the MBP coupling as a whole although only 50% of the bilayer surface is accessible to the protein, indicating a strong coupling between the two bilayer leaflets via the hydrophobic chain region. Moreover, the asymmetric coupling of MBP to the single supported bilayer does not result in a significant redistribution of lipids between the two bilayer leaflets. NMR relaxation time measurements in the headgroup and chain region of DMPG and DMPC suggest that the lateral diffusion coefficient of the acidic lipid decreases significantly due to the coupling with MBP while the zwitterionic DMPC is not affected.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
1151
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
127-36
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Interaction of myelin basic protein with single bilayers on a solid support: an NMR, DSC and polarized infrared ATR study.
pubmed:affiliation
Technische Universität München, Physik Department E22, Garching, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't