Abstract
We describe a method of measuring neutron scattering of aligned membranes with the momentum transfer oriented parallel or partly perpendicular to the plane of the membranes. The method obtains the complete information for the structures within fluid membranes obtainable by scattering. Data from alamethicin- and magainin-induced pores are presented. Although the in-plane scattering curves of these two peptides are similar to each other, their off-plane scattering patterns are strikingly distinct. Magainin pores exhibit intermembrane correlations.
Original language | English |
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Pages (from-to) | 641-645 |
Number of pages | 5 |
Journal | Biophysical Journal |
Volume | 75 |
Issue number | 2 |
DOIs | |
State | Published - Aug 1998 |
Externally published | Yes |
Funding
This work was supported by National Institutes of Health Grant GM55203 and Training Grant GM08280, and by the Robert A. Welch Foundation. We acknowledge the support of the NIST, U.S. Department of Commerce, in providing the neutron research facilities used in this work, which was also supported by the National Science Foundation under agreement no. DMR-942310, and of the IPNS, funded by the U.S. Department of Energy, BES-Materials Science, under contract W-31-109-Eng-38.
Funders | Funder number |
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BES-Materials | W-31-109-Eng-38 |
IPNS | |
Robert A. Welch Foundation | |
National Science Foundation | DMR-942310 |
National Institutes of Health | GM55203 |
U.S. Department of Energy | |
National Institute of General Medical Sciences | T32GM008280 |
National Institute of Standards and Technology | |
U.S. Department of Commerce |