Streptavidin two-dimensional (2D) crystals were grown on mica-supported phospholipid bilayers containing a biotinylated phospholipid. Their topography structure obtained by atomic force microscopy compares favorably with the electron microscopy analysis of streptavidin 2D crystals grown on lipid monolayers at the air-water interface. The streptavidin 2D crystals were used as a functionalized matrix for anchoring phospholipid bilayers on top of them. Biotinylated liposomes were found to bind specifically to the streptavidin matrix and to transform, locally, into flat lipid surfaces. Height measurements as well as parallel electron microscopy studies performed with biotinylated lipid tubules suggest that the flat lipid surfaces are indeed sin...
We present here some sensitive optical and mechanical experiments for monitoring the process of form...
Protein structure determination by classical x-ray crystallography requires three-dimensional crysta...
Two-dimensional crystals of a membrane protein, the proton ATPase from plant plasma membranes, have ...
Streptavidin two-dimensional (2D) crystals were grown on mica-supported phospholipid bilayers contai...
Streptavidin forms two-dimensional crystals when specifically bound to layers of biotinylated lipids...
Two-dimensional crystals of avidin were obtained on mixed lipid monolayers containing biotinylated l...
The development of functional supramolecular devices built by self-assembly of elementary molecules ...
We describe a rapid and convenient method of growing streptavidin (SA) monolayer crystals directly o...
A two-dimensional (2D) crystal of streptavidin has been obtained by a nonspecific binding method. Th...
Neutron reflection and surface plasmon optical experiments have been performed to evaluate structura...
To understand the effects of a crystalline protein layer on bilayer properties, we studied the mecha...
The biotin-binding protein streptavidin was crystallized as two-dimensional periodic arrays on bioti...
Protein structure determination by classical x-ray crystallography requires three-dimensional crysta...
AbstractProtein structure determination by classical x-ray crystallography requires three-dimensiona...
Theories of crystallization, both in 3-D and 2-D, are still very limited, mainly due to the scarcity...
We present here some sensitive optical and mechanical experiments for monitoring the process of form...
Protein structure determination by classical x-ray crystallography requires three-dimensional crysta...
Two-dimensional crystals of a membrane protein, the proton ATPase from plant plasma membranes, have ...
Streptavidin two-dimensional (2D) crystals were grown on mica-supported phospholipid bilayers contai...
Streptavidin forms two-dimensional crystals when specifically bound to layers of biotinylated lipids...
Two-dimensional crystals of avidin were obtained on mixed lipid monolayers containing biotinylated l...
The development of functional supramolecular devices built by self-assembly of elementary molecules ...
We describe a rapid and convenient method of growing streptavidin (SA) monolayer crystals directly o...
A two-dimensional (2D) crystal of streptavidin has been obtained by a nonspecific binding method. Th...
Neutron reflection and surface plasmon optical experiments have been performed to evaluate structura...
To understand the effects of a crystalline protein layer on bilayer properties, we studied the mecha...
The biotin-binding protein streptavidin was crystallized as two-dimensional periodic arrays on bioti...
Protein structure determination by classical x-ray crystallography requires three-dimensional crysta...
AbstractProtein structure determination by classical x-ray crystallography requires three-dimensiona...
Theories of crystallization, both in 3-D and 2-D, are still very limited, mainly due to the scarcity...
We present here some sensitive optical and mechanical experiments for monitoring the process of form...
Protein structure determination by classical x-ray crystallography requires three-dimensional crysta...
Two-dimensional crystals of a membrane protein, the proton ATPase from plant plasma membranes, have ...