- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1038/nmeth.1450
-
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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
- Copyright date:
- 2010
Journal article
A streptavidin variant with slower biotin dissociation and increased mechanostability.
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