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

Journal Article · Sat May 01 00:00:00 EDT 1993 · Langmuir; (United States)

DOI:https://doi.org/10.1021/la00029a003· OSTI ID:5845176

Vaknin, D ^[1]; Kjaer, K ^[2]; Ringsdorf, H; Blankenburg, R; Pipenstock, M; Diederich, A; Loesche, M ^[3]

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1. Ames Lab., IA (United States)
2. Risoe National Lab. (Denmark)
3. Univ. of Mainz (Germany)

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.

• DOE Contract Number: W-7405-ENG-82
• OSTI ID: 5845176
• Journal Information: Langmuir; (United States), Journal Name: Langmuir; (United States) Vol. 9:5; ISSN LANGD5; ISSN 0743-7463
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
400201* -- Chemical & Physicochemical Properties
550200 -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ADSORPTION
BARYONS
ELECTROMAGNETIC RADIATION
ELEMENTARY PARTICLES
FERMIONS
FILMS
HADRONS
INTERFACES
IONIZING RADIATIONS
LIPIDS
MEMBRANES
NEUTRONS
NUCLEONS
ORGANIC COMPOUNDS
PROTEINS
RADIATIONS
REFLECTION
SORPTION
THIN FILMS
X RADIATION