X-ray and neutron reflectivity studies of a protein monolayer adsorbed to a functionalized aqueous surface

We report the structural organization of a protein, streptavidin, specifically bound at aqueous surfaces to lipid monolayers functionalized by biotinylated head groups. X-ray and neutron reflectivity data with H[sub 2]O and D[sub 2]O as subphases are consistent with the formation of homogeneous mono...

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Bibliographic Details
Published in:Langmuir 1993-05, Vol.9 (5), p.1171-1174
Main Authors: Vaknin, David, Kjaer, Kristian, Ringsdorf, Helmut, Blankenburg, Rainer, Piepenstock, Michael, Diederich, Anke, Loesche, Mathias
Format: Article
Language:English
Subjects:
400201 - Chemical & Physicochemical Properties
550200 - Biochemistry
ADSORPTION
Artificial membranes and reconstituted systems
BARYONS
BASIC BIOLOGICAL SCIENCES
Biological and medical sciences
ELECTROMAGNETIC RADIATION
ELEMENTARY PARTICLES
FERMIONS
Fundamental and applied biological sciences. Psychology
HADRONS
INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY
INTERFACES
IONIZING RADIATIONS
LIPIDS
Membrane physicochemistry
MEMBRANES
Molecular biophysics
NEUTRONS
NUCLEONS
ORGANIC COMPOUNDS
PROTEINS
RADIATIONS
REFLECTION
SORPTION
THIN FILMS
X RADIATION
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Summary:We report the structural organization of a protein, streptavidin, specifically bound at aqueous surfaces to lipid monolayers functionalized by biotinylated head groups. X-ray and neutron reflectivity data with H[sub 2]O and D[sub 2]O as subphases are consistent with the formation of homogeneous monomolecular protein layers (thickness d[sub pr] [approx] 42 [+-] 2 [angstrom]) directly underneath the lipid. A new approach of analyzing all four data sets in terms of one general model reveals the dry volume of the protein, its average lateral density at the interface, and the amount of water interpenetrating the protein film. 24 refs., 3 figs., 1 tab.
ISSN:0743-7463
1520-5827
DOI:10.1021/la00029a003