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Backbone 1H, 15N and 13C resonance assignments of the 27kDa fluorescent protein mCherry.
Sette, Marco; Johnson, Laura Anne; Jimenez, Ralph; Mulder, Frans A A.
Affiliation
  • Sette M; Department of Chemical Sciences and Technology, University of Rome "Tor Vergata", Rome, Italy.
  • Johnson LA; CSPBAT Laboratory, Sorbonne Paris Cité, University of Paris 13, UMR 7244, CNRS, Bobigny, France.
  • Jimenez R; Department of Biochemistry, University of Colorado, 596 UCB, Boulder, CO, 80309, USA.
  • Mulder FAA; JILA, University of Colorado, and NIST, Boulder, CO, 80309, USA.
Biomol NMR Assign ; 17(2): 243-247, 2023 12.
Article in En | MEDLINE | ID: mdl-37684490
mCherry is one of the most successfully applied monomeric red fluorescent proteins (RFPs) for in vivo and in vitro imaging. However, questions pertaining to the photostability of the RFPs remain and rational further engineering of their photostability requires information about the fluorescence quenching mechanism in solution. To this end, NMR spectroscopic investigations might be helpful, and we present the near-complete backbone NMR chemical shift assignment to aid in this pursuit.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Engineering Language: En Journal: Biomol NMR Assign Journal subject: BIOLOGIA MOLECULAR / MEDICINA NUCLEAR Year: 2023 Document type: Article Affiliation country: Italy Country of publication: Netherlands
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Engineering Language: En Journal: Biomol NMR Assign Journal subject: BIOLOGIA MOLECULAR / MEDICINA NUCLEAR Year: 2023 Document type: Article Affiliation country: Italy Country of publication: Netherlands