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  1. Nature methods
  2. Year: 2006, Volume: 3
  3. Year: 2006, Volume: 3, Issue: 4
  4. A monovalent streptavidin with a single femtomolar biotin binding site
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A monovalent streptavidin with a single femtomolar biotin binding site
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A monovalent streptavidin with a single femtomolar biotin binding site

Content Provider PubMed Central
Author Howarth, Mark Chinnapen, Daniel J-f Kimberly, Gerrow Dorrestein, Pieter C. Grandy, Melanie R. Kelleher, Neil L. El-husseini, Alaa Ting, Alice Y.
Abstract 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 104-fold because part of the binding site comes from a neighboring subunit. Here we engineered a streptavidin tetramer with only one functional biotin binding subunit that retained the affinity, off rate and thermostability of wild-type streptavidin. In denaturant, we mixed a streptavidin variant containing three mutations that block biotin binding with wild-type streptavidin in a 3:1 ratio. Then we generated monovalent streptavidin by refolding and nickel-affinity purification. Similarly, we purified defined tetramers with two or three biotin binding subunits. Labeling of site-specifically biotinylated neuroligin-1 with monovalent streptavidin allowed stable neuroligin-1 tracking without cross-linking, whereas wild-type streptavidin aggregated neuroligin-1 and disrupted presynaptic contacts. Monovalent streptavidin should find general application in biomolecule labeling, single-particle tracking and nanotechnology.
Related Links http://dx.doi.org/10.1038/NMETHXXX
Starting Page 267
File Format PDF
ISSN 15487105
e-ISSN 15487105
Journal Nature methods
Issue Number 4
Volume Number 3
Language English
Publisher Date 2006-04-01
Access Restriction Open
Subject Keyword Research in Higher Education
Content Type Text
Resource Type Article
Subject Cell Biology Biochemistry Molecular Biology Biotechnology
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