Directed evolution of GFP with non-natural amino acids identifies residues for augmenting and photoswitching fluorescence† †Electronic supplementary information (ESI) available: Detailed experimental methods, supplementary Fig. 1 to 11 and supplementary Tables 1–3. See DOI: 10.1039/c4sc02827a Click here for additional data file.

نویسندگان

  • Samuel C. Reddington
  • Amy J. Baldwin
  • Rebecca Thompson
  • Andrea Brancale
  • Eric M. Tippmann
  • D. Dafydd Jones
چکیده

School of Biosciences, Cardiff University, C cardiff.ac.uk; Tel: +44 (0)29 20874290 School of Chemistry, Cardiff University, Ca School of Pharmacy and Pharmaceutical Sc † Electronic supplementary information methods, supplementary Fig. 1 to 11 an 10.1039/c4sc02827a ‡ SCR and AJB contributed equally to this § Current address: Dept of Biochemistry, { Current address: Astbury Centre for Stru k Current address: Department of Chem Wayne, Fort Wayne, IN 46815, USA. Cite this: Chem. Sci., 2015, 6, 1159

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منابع مشابه

Functional modulation and directed assembly of an enzyme through designed non-natural post-translation modification† †Electronic supplementary information (ESI) available: Detailed experimental methods, supplementary Fig. 1 to 11 and supplementary Tables 1 to 3. See DOI: 10.1039/c4sc03900a Click here for additional data file. Click here for additional data file.

Post-translational modification (PTM) modulates and supplements protein functionality. In nature this high precision event requires specific motifs and/or associated modification machinery. To overcome the inherent complexity that hinders PTM's wider use, we have utilized a non-native biocompatible Click chemistry approach to site-specifically modify TEM b-lactamase that adds new functionality....

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عنوان ژورنال:

دوره 6  شماره 

صفحات  -

تاریخ انتشار 2015