TY - JOUR KW - Biochemistry KW - Structural Biology AU - Marco Sette AU - Laura Johnson AU - Ralph Jimenez AU - Frans Mulder AB -

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.

BT - Biomolecular NMR Assignments DA - 2024-02 DO - 10.1007/s12104-023-10149-z IS - 2 N2 -

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.

PB - Springer Science and Business Media LLC PY - 2023 SP - 243 EP - 247 T2 - Biomolecular NMR Assignments TI - Backbone 1H, 15N and 13C resonance assignments of the 27kDa fluorescent protein mCherry VL - 17 SN - 1874-2718, 1874-270X ER -