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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.

Original publication

DOI

10.1038/nmeth.1450

Type

Journal article

Journal

Nat Methods

Publication Date

05/2010

Volume

7

Pages

391 - 393

Keywords

Biomechanical Phenomena, Biotin, Biotinylation, Escherichia coli Proteins, Membrane Proteins, Microscopy, Atomic Force, Molecular Sequence Data, Protein Binding, Protein Engineering, Streptavidin