The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures (Q28305719)

6

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author name string

Anders Holmberg

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Anna Blomstergren

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Olof Nord

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Morten Lukacs

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Joakim Lundeberg

Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation

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language of work or name

English

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publication date

February 2005

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published in

Electrophoresis

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volume

26

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issue

3

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page(s)

501-10

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cites work

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Extremely high thermal stability of streptavidin and avidin upon biotin binding

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A structural snapshot of an intermediate on the streptavidin-biotin dissociation pathway

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Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex

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Temperature Control of Biotin Binding and Release with A Streptavidin-Poly(N-isopropylacrylamide) Site-Specific Conjugate

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Structural origins of high-affinity biotin binding to streptavidin

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Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation

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Avidin and streptavidin

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Solid-phase method for the purification of DNA sequencing reactions

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Reversibility of biotin-binding by selective modification of tyrosine in avidin

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Site-specific polymer-streptavidin bioconjugate for pH-controlled binding and triggered release of biotin

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Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin

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Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120

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Energetic roles of hydrogen bonds at the ureido oxygen binding pocket in the streptavidin-biotin complex

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Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin system

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