A monovalent streptavidin with a single femtomolar biotin binding site

Streptavidin and avidin are used ubiquitously because of the remarkable affinity of their biotin binding, but they are tetramers, which disrupts many of their applications. Making either protein monomeric reduces affinity by at least 10 4 -fold because part of the binding site comes from a neighbori...

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Veröffentlicht in:	Nature methods 2006-04, Vol.3 (4), p.267-273
Hauptverfasser:	Ting, Alice Y, Howarth, Mark, Chinnapen, Daniel J-F, Gerrow, Kimberly, Dorrestein, Pieter C, Grandy, Melanie R, Kelleher, Neil L, El-Husseini, Alaa
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Bioinformatics Biological Microscopy Biological Techniques Biomedical and Life Sciences Biomedical Engineering/Biotechnology Biotin Biotin - chemistry Biotin - metabolism Biotinylation Cell Adhesion Molecules, Neuronal Cross-Linking Reagents - pharmacology Hippocampus - cytology Hippocampus - ultrastructure Hybridization Kinetics Life Sciences Membrane Proteins - metabolism Molecular probes Mutagenesis, Site-Directed Mutation Nanotechnology Nanotechnology - methods Nerve Tissue Proteins - metabolism Neurons - metabolism Nickel Physiological aspects Protein Denaturation Protein Engineering - methods Protein Folding Proteins Proteomics Streptavidin - chemistry Streptavidin - metabolism Synapses - metabolism Temperature Vitamin B
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