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A streptavidin variant with slower biotin dissociation and increased mechanostability.

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 tra...

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Publication status:
Published

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Publisher copy:
10.1038/nmeth.1450

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
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Journal:
Nature methods
Volume:
7
Issue:
5
Pages:
391-393
Publication date:
2010-05-05
DOI:
EISSN:
1548-7105
ISSN:
1548-7091
URN:
uuid:68fc5cc6-acfc-4fc4-bf40-8c6ea66038fa
Source identifiers:
99880
Local pid:
pubs:99880

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