Cargando…

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

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 quen...

Descripción completa

Detalles Bibliográficos
Autores principales: Sette, Marco, Johnson, Laura Anne, Jimenez, Ralph, Mulder, Frans A.A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10630242/
https://www.ncbi.nlm.nih.gov/pubmed/37684490
http://dx.doi.org/10.1007/s12104-023-10149-z
_version_ 1785146007818862592
author Sette, Marco
Johnson, Laura Anne
Jimenez, Ralph
Mulder, Frans A.A.
author_facet Sette, Marco
Johnson, Laura Anne
Jimenez, Ralph
Mulder, Frans A.A.
author_sort Sette, Marco
collection PubMed
description 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.
format Online
Article
Text
id pubmed-10630242
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher Springer Netherlands
record_format MEDLINE/PubMed
spelling pubmed-106302422023-11-14 Backbone (1)H, (15)N and (13)C resonance assignments of the 27kDa fluorescent protein mCherry Sette, Marco Johnson, Laura Anne Jimenez, Ralph Mulder, Frans A.A. Biomol NMR Assign Article 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. Springer Netherlands 2023-09-09 2023 /pmc/articles/PMC10630242/ /pubmed/37684490 http://dx.doi.org/10.1007/s12104-023-10149-z Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Sette, Marco
Johnson, Laura Anne
Jimenez, Ralph
Mulder, Frans A.A.
Backbone (1)H, (15)N and (13)C resonance assignments of the 27kDa fluorescent protein mCherry
title Backbone (1)H, (15)N and (13)C resonance assignments of the 27kDa fluorescent protein mCherry
title_full Backbone (1)H, (15)N and (13)C resonance assignments of the 27kDa fluorescent protein mCherry
title_fullStr Backbone (1)H, (15)N and (13)C resonance assignments of the 27kDa fluorescent protein mCherry
title_full_unstemmed Backbone (1)H, (15)N and (13)C resonance assignments of the 27kDa fluorescent protein mCherry
title_short Backbone (1)H, (15)N and (13)C resonance assignments of the 27kDa fluorescent protein mCherry
title_sort backbone (1)h, (15)n and (13)c resonance assignments of the 27kda fluorescent protein mcherry
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10630242/
https://www.ncbi.nlm.nih.gov/pubmed/37684490
http://dx.doi.org/10.1007/s12104-023-10149-z
work_keys_str_mv AT settemarco backbone1h15nand13cresonanceassignmentsofthe27kdafluorescentproteinmcherry
AT johnsonlauraanne backbone1h15nand13cresonanceassignmentsofthe27kdafluorescentproteinmcherry
AT jimenezralph backbone1h15nand13cresonanceassignmentsofthe27kdafluorescentproteinmcherry
AT mulderfransaa backbone1h15nand13cresonanceassignmentsofthe27kdafluorescentproteinmcherry