We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
A streptavidin variant with slower biotin dissociation and increased mechanostability.
- Authors
Chivers, Claire E; Crozat, Estelle; Chu, Calvin; Moy, Vincent T; Sherratt, David J; Howarth, Mark
- Abstract
Streptavidin binds biotin conjugates with exceptional stability but dissociation does occur, limiting its use in imaging, DNA amplification and nanotechnology. We identified a mutant streptavidin, traptavidin, with more than tenfold slower biotin dissociation, increased mechanical strength and improved thermostability; this resilience should enable diverse applications. FtsK, a motor protein important in chromosome segregation, rapidly displaced streptavidin from biotinylated DNA, whereas traptavidin resisted displacement, indicating the force generated by Ftsk translocation.
- Publication
Nature methods, 2010, Vol 7, Issue 5, p391
- ISSN
1548-7105
- Publication type
Journal Article
- DOI
10.1038/nmeth.1450