Abstract
Recombinant proteins bearing a tag are crucial tools for assessing protein location or function. Small tags such as Cys4 tag (tetracysteine; Cys-Cys-X-X-Cys-Cys) are less likely disrupt protein function in the living cell than green fluorescent protein. Herein we report the first example of the design and synthesis of a dual fluorescence and hyperpolarized (129)Xe NMR-based sensor of Cys4-tagged proteins. This sensor becomes fluorescent when bound to such Cys4-tagged peptides, and the (129)Xe NMR spectrum exhibits a specific signal, characteristic of the biosensor-peptide association.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Biosensing Techniques
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Cysteine / analysis*
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Fluoresceins / chemistry*
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Fluorescent Dyes / chemistry*
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Organometallic Compounds / chemistry*
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Peptides / analysis*
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Polycyclic Compounds / chemistry*
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Recombinant Proteins / analysis
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Spectrometry, Fluorescence
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Xenon Isotopes / chemistry
Substances
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CrAsH compound
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Fluoresceins
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Fluorescent Dyes
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Organometallic Compounds
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Peptides
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Polycyclic Compounds
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Recombinant Proteins
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Xenon Isotopes
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cryptophane
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6-carboxyfluorescein
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Cysteine