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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2023
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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 |
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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 |
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