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

Marco Sette; Laura Anne Johnson; Ralph Jimenez; Frans A A Mulder

doi:10.1007/s12104-023-10149-z

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

Biomol NMR Assign. 2023 Dec;17(2):243-247. doi: 10.1007/s12104-023-10149-z. Epub 2023 Sep 9.

Authors

Marco Sette^{1

2}, Laura Anne Johnson³, Ralph Jimenez^{4

5}, Frans A A Mulder^{6

7}

Affiliations

¹ Department of Chemical Sciences and Technology, University of Rome "Tor Vergata", Rome, Italy.
² CSPBAT Laboratory, Sorbonne Paris Cité, University of Paris 13, UMR 7244, CNRS, Bobigny, France.
³ Department of Biochemistry, University of Colorado, 596 UCB, Boulder, CO, 80309, USA.
⁴ JILA, University of Colorado, and NIST, Boulder, CO, 80309, USA.
⁵ Department of Chemistry, University of Colorado, 215 UCB, Boulder, CO, 80309, USA.
⁶ Interdisciplinary Nanoscience Center iNANO and Department of Chemistry, University of Aarhus, Aarhus, 8000, Denmark. fmulder@chem.au.dk.
⁷ Institute of Biochemistry, Johannes Kepler Universität Linz, Linz, 4040, Austria. fmulder@chem.au.dk.

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.

Keywords: Chemical shift; Photostability; Protein engineering; Red fluorescent protein; mCherry.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Nuclear Magnetic Resonance, Biomolecular
Protein Engineering* / methods