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Title: NMR Investigations of Sphingomyelin/Cholesterol Lipid Bilayers.

Abstract

Abstract not provided.

Authors:
Publication Date:
Research Org.:
Sandia National Lab. (SNL-NM), Albuquerque, NM (United States)
Sponsoring Org.:
USDOE National Nuclear Security Administration (NNSA)
OSTI Identifier:
1157527
Report Number(s):
SAND2007-1879C
523657
DOE Contract Number:
AC04-94AL85000
Resource Type:
Conference
Resource Relation:
Conference: Proposed for presentation at the 50th New Mexico Regional NMR (Nuclear Magnetic Resonance) Meeting held May 5, 2007 in Albuquerque, NM.
Country of Publication:
United States
Language:
English

Citation Formats

Costello, Alison Leslie. NMR Investigations of Sphingomyelin/Cholesterol Lipid Bilayers.. United States: N. p., 2007. Web.
Costello, Alison Leslie. NMR Investigations of Sphingomyelin/Cholesterol Lipid Bilayers.. United States.
Costello, Alison Leslie. Thu . "NMR Investigations of Sphingomyelin/Cholesterol Lipid Bilayers.". United States. doi:. https://www.osti.gov/servlets/purl/1157527.
@article{osti_1157527,
title = {NMR Investigations of Sphingomyelin/Cholesterol Lipid Bilayers.},
author = {Costello, Alison Leslie},
abstractNote = {Abstract not provided.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Thu Mar 01 00:00:00 EST 2007},
month = {Thu Mar 01 00:00:00 EST 2007}
}

Conference:
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  • Abstract not provided.
  • Partitioning of small hydrophobic molecules into lipid bilayers containing cholesterol has been studied using the 2XC diffractometer at the University of Missouri Research Reactor. Locations of the compounds were determined by Fourier difference methods with data from both deuterated and undeuterated compounds introduced into the bilayers from the vapor phase. Data fitting procedures were developed for determining how well the compounds were localized. The compounds were found to be localized in a narrow region at the center of the hydrophobic layer, between the two halves of the bilayer. The structures are therefore intercalated structures with the long axis of themore » molecules in the plane of the bilayer.« less
  • Membrane raft size measurements are crucial to understanding the stability and functionality of rafts in cells. The challenge of accurately measuring raft size is evidenced by the disparate reports of domain sizes, which range from nanometers to microns for the ternary model membrane system sphingomyelin (SM)/1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC)/cholesterol (Chol). Using F rster resonance energy transfer (FRET) and differential scanning calorimetry (DSC), we established phase diagrams for porcine brain SM (bSM)/dioleoyl-sn-glycero-3-phosphocholine (DOPC)/Chol and bSM/POPC/Chol at 15 and 25 C. By combining two techniqueswith different spatial sensitivities, namely FRET and small-angle neutron scattering (SANS),we have significantly narrowed the uncertainty in domain size estimatesmore » for bSM/POPC/Chol mixtures. Compositional trends in FRET data revealed coexisting domains at 15 and 25 C for bothmixtures, while SANS measurements detected no domain formation for bSM/POPC/Chol. Together these results indicate that liquid domains in bSM/POPC/Chol are between 2 and 7 nmin radius at 25 C: that is, domains must be on the order of the 2 6 nmF rster distance of the FRET probes, but smaller than the ~7 nm minimum cluster size detectable with SANS. However, for palmitoyl SM (PSM)/POPC/Chol at a similar composition, SANS detected coexisting liquid domains. This increase in domain size upon replacing the natural SMcomponent (which consists of amixture of chain lengths) with synthetic PSM, suggests a role for SM chain length in modulating raft size in vivo.« less
  • Abstract not provided.