Backbone 1H, 15N and 13C resonance assignments of the 27kDa fluorescent protein mCherry
Year: 2023
Type: 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.
Source: Biomolecular NMR Assignments
Authors: Marco Sette, Laura Anne Johnson, Ralph Jimenez, Frans A.A. Mulder
Institutions: University of Rome Tor Vergata, Centre National de la Recherche Scientifique, Sorbonne Paris Cité, Chimie, Structures et Propriétés de Biomatériaux et d'Agents Thérapeutiques, University of Colorado Boulder, University of Colorado System, Joint Institute for Laboratory Astrophysics, Johannes Kepler University of Linz, Aarhus University
Language: English
Subfield: Spectroscopy
Field: Chemistry
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,390
OpenAlex ID: W4386531832