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Backbone H, N and C resonance assignments of the 27kDa fluorescent protein mCherry. | LitMetric

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

Biomol NMR Assign

Interdisciplinary Nanoscience Center iNANO and Department of Chemistry, University of Aarhus, Aarhus, 8000, Denmark.

Published: December 2023

AI Article Synopsis

  • mCherry is a widely used red fluorescent protein for both live and lab imaging, but concerns about its long-term stability under light exposure persist.
  • Understanding how its fluorescence diminishes (quenching) in solution is crucial for improving its photostability through engineering.
  • The text presents near-complete NMR chemical shift assignments that could assist researchers in investigating these quenching mechanisms further.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10630242PMC
http://dx.doi.org/10.1007/s12104-023-10149-zDOI Listing

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