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Chem Commun (Camb) ; 51(57): 11482-4, 2015 Jul 21.
Article in English | MEDLINE | ID: mdl-26091539

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.


Subject(s)
Cysteine/analysis , Fluoresceins/chemistry , Fluorescent Dyes/chemistry , Organometallic Compounds/chemistry , Peptides/analysis , Polycyclic Compounds/chemistry , Amino Acid Sequence , Biosensing Techniques , Molecular Sequence Data , Nuclear Magnetic Resonance, Biomolecular , Recombinant Proteins/analysis , Spectrometry, Fluorescence , Xenon Isotopes/chemistry
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