Two-dimensional crystals of avidin were obtained on mixed lipid monolayers containing biotinylated lipids (N-biotinyl-dipalmitoyl-L-alpha-phosphatidyl ethanolamine and dioleoyl phosphatidyl choline) by specific interaction. Image analysis of electron micrographs of these crystals revealed p2 symmetry with the unit cell parameters a = 66 +/- 2 A, b = 68 +/- 1 A, and gamma = 121 +/- 4 degrees. The projection map showed, at a resolution of about 27 A, that the four subunits within one avidin molecule are separated into two parts. Comparison between avidin and streptavidin reveals that avidin molecule binds to the lipid monolayer in an orientation similar to that of streptavidin
Similar to streptavidin, the binding of biotin by avidin does not appear to be cooperative in the tr...
A comparison of the binding properties of avidin, streptavidin, neutrAvidin, and antibiotin antibody...
Avidin (Avd) is a protein first discovered in chicken egg white, and later in other birds, reptiles,...
Two-dimensional crystals of avidin were obtained on mixed lipid monolayers containing biotinylated l...
Streptavidin forms two-dimensional crystals when specifically bound to layers of biotinylated lipids...
Fourier-transform infrared studies have been carried out to investigate the secondary structure and ...
The biotin-binding protein streptavidin was crystallized as two-dimensional periodic arrays on bioti...
AbstractThe crystal structure of the complex formed between the egg-white biotin-binding protein, av...
AbstractThe interaction of avidin – a basic protein from hen egg-white – with dimyristoyl-phosphatid...
The specific binding of hen egg white avidin to phosphatidylcholine lipid membranes containing spin-...
Streptavidin two-dimensional (2D) crystals were grown on mica-supported phospholipid bilayers contai...
Avidin is a homotetrameric protein known for its high binding affinity and specificity for biotin wh...
Streptavidin two-dimensional (2D) crystals were grown on mica-supported phospholipid bilayers contai...
SummaryBiotin-(strept)avidin complex is widely used in biotechnology because of its extremely high b...
A two-dimensional (2D) crystal of streptavidin has been obtained by a nonspecific binding method. Th...
Similar to streptavidin, the binding of biotin by avidin does not appear to be cooperative in the tr...
A comparison of the binding properties of avidin, streptavidin, neutrAvidin, and antibiotin antibody...
Avidin (Avd) is a protein first discovered in chicken egg white, and later in other birds, reptiles,...
Two-dimensional crystals of avidin were obtained on mixed lipid monolayers containing biotinylated l...
Streptavidin forms two-dimensional crystals when specifically bound to layers of biotinylated lipids...
Fourier-transform infrared studies have been carried out to investigate the secondary structure and ...
The biotin-binding protein streptavidin was crystallized as two-dimensional periodic arrays on bioti...
AbstractThe crystal structure of the complex formed between the egg-white biotin-binding protein, av...
AbstractThe interaction of avidin – a basic protein from hen egg-white – with dimyristoyl-phosphatid...
The specific binding of hen egg white avidin to phosphatidylcholine lipid membranes containing spin-...
Streptavidin two-dimensional (2D) crystals were grown on mica-supported phospholipid bilayers contai...
Avidin is a homotetrameric protein known for its high binding affinity and specificity for biotin wh...
Streptavidin two-dimensional (2D) crystals were grown on mica-supported phospholipid bilayers contai...
SummaryBiotin-(strept)avidin complex is widely used in biotechnology because of its extremely high b...
A two-dimensional (2D) crystal of streptavidin has been obtained by a nonspecific binding method. Th...
Similar to streptavidin, the binding of biotin by avidin does not appear to be cooperative in the tr...
A comparison of the binding properties of avidin, streptavidin, neutrAvidin, and antibiotin antibody...
Avidin (Avd) is a protein first discovered in chicken egg white, and later in other birds, reptiles,...