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Effect of sequential C‐terminal tryptophans on green fluorescent protein fluorescence
The effect of the addition of sequential C‐terminal tryptophan residues on the fluorescence intensity of GFP was investigated. Tandem repeats of six tryptophan residues markedly decreased fluorescence intensity. This phenomenon is likely to occur because of the inhibition of GFP folding, resulting i...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6026694/ https://www.ncbi.nlm.nih.gov/pubmed/29988552 http://dx.doi.org/10.1002/2211-5463.12445 |
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author | Tsuchida, Shirou Kanashiki, Takumi Izumiya, Shuhei Ichikawa, Takuya Kurosawa, Ryusuke Hamaue, Naoya Aoki, Takashi |
author_facet | Tsuchida, Shirou Kanashiki, Takumi Izumiya, Shuhei Ichikawa, Takuya Kurosawa, Ryusuke Hamaue, Naoya Aoki, Takashi |
author_sort | Tsuchida, Shirou |
collection | PubMed |
description | The effect of the addition of sequential C‐terminal tryptophan residues on the fluorescence intensity of GFP was investigated. Tandem repeats of six tryptophan residues markedly decreased fluorescence intensity. This phenomenon is likely to occur because of the inhibition of GFP folding, resulting in insolubility. Exploiting this phenomenon, we constructed a cloning vector that facilitates the identification of recombinant colonies of Escherichia coli by the activation of GFP. |
format | Online Article Text |
id | pubmed-6026694 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-60266942018-07-09 Effect of sequential C‐terminal tryptophans on green fluorescent protein fluorescence Tsuchida, Shirou Kanashiki, Takumi Izumiya, Shuhei Ichikawa, Takuya Kurosawa, Ryusuke Hamaue, Naoya Aoki, Takashi FEBS Open Bio Methods The effect of the addition of sequential C‐terminal tryptophan residues on the fluorescence intensity of GFP was investigated. Tandem repeats of six tryptophan residues markedly decreased fluorescence intensity. This phenomenon is likely to occur because of the inhibition of GFP folding, resulting in insolubility. Exploiting this phenomenon, we constructed a cloning vector that facilitates the identification of recombinant colonies of Escherichia coli by the activation of GFP. John Wiley and Sons Inc. 2018-05-29 /pmc/articles/PMC6026694/ /pubmed/29988552 http://dx.doi.org/10.1002/2211-5463.12445 Text en © 2018 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Methods Tsuchida, Shirou Kanashiki, Takumi Izumiya, Shuhei Ichikawa, Takuya Kurosawa, Ryusuke Hamaue, Naoya Aoki, Takashi Effect of sequential C‐terminal tryptophans on green fluorescent protein fluorescence |
title | Effect of sequential C‐terminal tryptophans on green fluorescent protein fluorescence |
title_full | Effect of sequential C‐terminal tryptophans on green fluorescent protein fluorescence |
title_fullStr | Effect of sequential C‐terminal tryptophans on green fluorescent protein fluorescence |
title_full_unstemmed | Effect of sequential C‐terminal tryptophans on green fluorescent protein fluorescence |
title_short | Effect of sequential C‐terminal tryptophans on green fluorescent protein fluorescence |
title_sort | effect of sequential c‐terminal tryptophans on green fluorescent protein fluorescence |
topic | Methods |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6026694/ https://www.ncbi.nlm.nih.gov/pubmed/29988552 http://dx.doi.org/10.1002/2211-5463.12445 |
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