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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




Journal article


Nat Methods

Publication Date





391 - 393


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