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Nat Methods. 2010 May;7(5):391-3. doi: 10.1038/nmeth.1450. Epub 2010 Apr 11.

A streptavidin variant with slower biotin dissociation and increased mechanostability.

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  • 1Department of Biochemistry, Oxford University, UK.


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.

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