help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

Biophysical Journal 59: 1325-1332 (1991)
© 1991 the Biophysical Society

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vaknin, D.
Right arrow Articles by Lösche, M.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Vaknin, D.
Right arrow Articles by Lösche, M.

Structural properties of phosphatidylcholine in a monolayer at the air/water interface

Neutron reflection study and reexamination of x-ray reflection measurements

David Vaknin *, Kristian Kjaer *, Jens Als-Nielsen * and Mathias Lösche {ddagger}

Physics Department, Risø National Laboratory, DK-4000 Roskilde, Denmark
Institute of Physical Chemistry, Johannes-Gutenberg-Universität Mainz, D-6500 Mainz, Germany

ABSTRACT

Neutron reflectivities of phosphatidylcholine monolayers in the liquid condensed (LC) phase on ultrapure H2O and D2O subphases have been measured on a Langmuir film balance. Using a dedicated liquid surface reflectometer, reflectivities down to R = 10-6 in the momentum transfer range Qz = 0-0.4 Å-1 were accessed.

In a new approach, by refining neutron reflectivity data from chain-perdeuterated DPPC-d62 in combination with x-ray measurements on the same monolayer under similar conditions it is shown that the two techniques mutually complement one another. This analysis leads to a detailed conception of the interface structure. It is found that in the LC phase (which is analogous to the Lß, phase in vesicle dispersions) the head group is interpenetrated with subphase water (4 ± 2.5 molecules per lipid) and the average tilt angle of the hydrophobic chains from the surface normal is 33 ± 3 degrees.




This article has been cited by other articles:


Home page
Biophys. JHome page
M. D. Lad, F. Birembaut, L. A. Clifton, R. A. Frazier, J. R. P. Webster, and R. J. Green
Antimicrobial Peptide-Lipid Binding Interactions and Binding Selectivity
Biophys. J., May 15, 2007; 92(10): 3575 - 3586.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1991 by the Biophysical Society.