| Literature DB >> 26091539 |
N Kotera1, E Dubost, G Milanole, E Doris, E Gravel, N Arhel, T Brotin, J-P Dutasta, J Cochrane, E Mari, C Boutin, E Léonce, P Berthault, B Rousseau.
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.Entities:
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Year: 2015 PMID： 26091539 DOI： 10.1039/c5cc04721h
Source DB: PubMed Journal: Chem Commun (Camb) ISSN： 1359-7345 Impact factor: 6.222