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

Marco Sette, Laura Anne Johnson, Ralph Jimenez, Frans A A Mulder^*

^*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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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.

Original language	English
Journal	Biomolecular NMR Assignments
Volume	17
Issue	2
Pages (from-to)	243-247
Number of pages	5
ISSN	1874-2718
DOIs	https://doi.org/10.1007/s12104-023-10149-z
Publication status	Published - Dec 2023

Keywords

Chemical shift
Photostability
Protein engineering
Red fluorescent protein
mCherry
Protein Engineering/methods
Nuclear Magnetic Resonance, Biomolecular

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s12104-023-10149-zFinal published version, 2.43 MBLicence: CC BY

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

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, Protein Engineering/methods, Nuclear Magnetic Resonance, Biomolecular",

author = "Marco Sette and Johnson, {Laura Anne} and Ralph Jimenez and Mulder, {Frans A A}",

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AU - Sette, Marco

AU - Johnson, Laura Anne

AU - Jimenez, Ralph

AU - Mulder, Frans A A

PY - 2023/12

Y1 - 2023/12

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.

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.

KW - Chemical shift

KW - Photostability

KW - Protein engineering

KW - Red fluorescent protein

KW - mCherry

KW - Protein Engineering/methods

KW - Nuclear Magnetic Resonance, Biomolecular

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U2 - 10.1007/s12104-023-10149-z

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JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

IS - 2

ER -

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

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Keywords

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