ArticleBiophysical journal1993
Influence of surface chemistry on the structural organization of monomolecular protein layers adsorbed to functionalized aqueous interfaces.
Article in Biophysical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 45 citations in OpenAlex.
- Zooming in on disordered systems: neutron reflection studies of proteins associated with fluid membranes.Biochimica et biophysica acta · 2014Review
- An ion-channel-containing model membrane: structural determination by magnetic contrast neutron reflectometry.Soft matter · 2009Article
- A model membrane protein for binding volatile anesthetics.Biophysical journal · 2004Article
- Comparative structural studies of Vpu peptides in phospholipid monolayers by x-ray scattering.Biophysical journal · 2003Article
- Hydration state of single cytochrome c monolayers on soft interfaces via neutron interferometry.Biophysical journal · 2001Article
- Structural studies of the HIV-1 accessory protein Vpu in langmuir monolayers: synchrotron X-ray reflectivity.Biophysical journal · 2001Article
- Urease and hexadecylamine-urease films at the air-water interface: an x-ray reflection and grazing incidence x-ray diffraction study.Biophysical journal · 1999Article
- Bacterial S-layer protein coupling to lipids: x-ray reflectivity and grazing incidence diffraction studies.Biophysical journal · 1999Article
- Electron crystallographic analysis of two-dimensional streptavidin crystals coordinated to metal-chelated lipid monolayers.Biophysical journal · 1998Article
- Hybrid bilayer membranes in air and water: infrared spectroscopy and neutron reflectivity studies.Biophysical journal · 1998Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular organization of streptavidin (SA) bound to aqueous surface monolayers of biotin-functionalized lipids and binary lipid mixtures has been investigated with neutron reflectivity and electron and fluorescence microscopy. The substitution of deuterons (2H) for protons (1H), both in subphase water molecules and in the alkyl chains of the lipid surface monolayer, was utilized to determine the interface structure on the molecular length scale. In all cases studied, the protein forms monomolecular layers underneath the interface with thickness values of approximately 40 A. A systematic dependence of the structural properties of such self-assembled SA monolayers on the surface chemistry was observed: the lateral protein density depends on the length of the spacer connecting the biotin moiety and its hydrophobic anchor. The hydration of the lipid head groups in the protein-bound state depends on the dipole moment density at the interface.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.