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 -