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Backbone 1H, 15N and 13C resonance assignments of the 27kDa fluorescent protein mCherry.


ABSTRACT: 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.

SUBMITTER: Sette M 

PROVIDER: S-EPMC10630242 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature

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Backbone <sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C resonance assignments of the 27kDa fluorescent protein mCherry.

Sette Marco M   Johnson Laura Anne LA   Jimenez Ralph R   Mulder Frans A A FAA  

Biomolecular NMR assignments 20230909 2


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. ...[more]

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