Fluorescence Dynamics of N-Terminal Tryptofan-X Residues in Polypeptide: pH Response
The influence of the second amino acid on the pH response of the genetically encoded pH indicators is studied. The second Trp has been substituted by Ala and Glu to reduce self-quenching. Compared with the previously reported Trp-Trp-Ala-Ser (WWAS), the two new tetrapeptides, Trp-Ala-Ala-Ser (WAAS)...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Li, L. [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer Science+Business Media, LLC 2017 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of applied spectroscopy - Springer US, 1966, 84(2017), 4 vom: Sept., Seite 633-638 |
|---|---|
| Übergeordnetes Werk: |
volume:84 ; year:2017 ; number:4 ; month:09 ; pages:633-638 |
| Links: |
|---|
| DOI / URN: |
10.1007/s10812-017-0521-4 |
|---|
| Katalog-ID: |
OLC2034688082 |
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| 520 | |a The influence of the second amino acid on the pH response of the genetically encoded pH indicators is studied. The second Trp has been substituted by Ala and Glu to reduce self-quenching. Compared with the previously reported Trp-Trp-Ala-Ser (WWAS), the two new tetrapeptides, Trp-Ala-Ala-Ser (WAAS) and Trp-Glu-Ala-Ser (WEAS), have higher fluorescence quantum yields, longer fluorescence lifetimes, and more sensitive pH responses. As novel genetically encoded pH indicators, the N-terminal Trp-Ala and Trp-Glu could be fused to proteins for monitoring the environmental pH values during the studies of functional proteins. | ||
| 650 | 4 | |a fluorescent sensor | |
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| 700 | 1 | |a Pan, H. |4 aut | |
| 700 | 1 | |a Chen, J. |4 aut | |
| 700 | 1 | |a Xu, J. |4 aut | |
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10.1007/s10812-017-0521-4 doi (DE-627)OLC2034688082 (DE-He213)s10812-017-0521-4-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Li, L. verfasserin aut Fluorescence Dynamics of N-Terminal Tryptofan-X Residues in Polypeptide: pH Response 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC 2017 The influence of the second amino acid on the pH response of the genetically encoded pH indicators is studied. The second Trp has been substituted by Ala and Glu to reduce self-quenching. Compared with the previously reported Trp-Trp-Ala-Ser (WWAS), the two new tetrapeptides, Trp-Ala-Ala-Ser (WAAS) and Trp-Glu-Ala-Ser (WEAS), have higher fluorescence quantum yields, longer fluorescence lifetimes, and more sensitive pH responses. As novel genetically encoded pH indicators, the N-terminal Trp-Ala and Trp-Glu could be fused to proteins for monitoring the environmental pH values during the studies of functional proteins. fluorescent sensor genetically encoded pH indicator Trp-Ala-Ala-Ser Trp-Glu-Ala-Ser Trp-Trp-Ala-Ser Cao, X. aut Zhou, Zh. aut Zhang, S. aut Pan, H. aut Chen, J. aut Xu, J. aut Enthalten in Journal of applied spectroscopy Springer US, 1966 84(2017), 4 vom: Sept., Seite 633-638 (DE-627)129972495 (DE-600)410515-1 (DE-576)015535800 0021-9037 nnns volume:84 year:2017 number:4 month:09 pages:633-638 https://doi.org/10.1007/s10812-017-0521-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 AR 84 2017 4 09 633-638 |
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10.1007/s10812-017-0521-4 doi (DE-627)OLC2034688082 (DE-He213)s10812-017-0521-4-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Li, L. verfasserin aut Fluorescence Dynamics of N-Terminal Tryptofan-X Residues in Polypeptide: pH Response 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC 2017 The influence of the second amino acid on the pH response of the genetically encoded pH indicators is studied. The second Trp has been substituted by Ala and Glu to reduce self-quenching. Compared with the previously reported Trp-Trp-Ala-Ser (WWAS), the two new tetrapeptides, Trp-Ala-Ala-Ser (WAAS) and Trp-Glu-Ala-Ser (WEAS), have higher fluorescence quantum yields, longer fluorescence lifetimes, and more sensitive pH responses. As novel genetically encoded pH indicators, the N-terminal Trp-Ala and Trp-Glu could be fused to proteins for monitoring the environmental pH values during the studies of functional proteins. fluorescent sensor genetically encoded pH indicator Trp-Ala-Ala-Ser Trp-Glu-Ala-Ser Trp-Trp-Ala-Ser Cao, X. aut Zhou, Zh. aut Zhang, S. aut Pan, H. aut Chen, J. aut Xu, J. aut Enthalten in Journal of applied spectroscopy Springer US, 1966 84(2017), 4 vom: Sept., Seite 633-638 (DE-627)129972495 (DE-600)410515-1 (DE-576)015535800 0021-9037 nnns volume:84 year:2017 number:4 month:09 pages:633-638 https://doi.org/10.1007/s10812-017-0521-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 AR 84 2017 4 09 633-638 |
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10.1007/s10812-017-0521-4 doi (DE-627)OLC2034688082 (DE-He213)s10812-017-0521-4-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Li, L. verfasserin aut Fluorescence Dynamics of N-Terminal Tryptofan-X Residues in Polypeptide: pH Response 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC 2017 The influence of the second amino acid on the pH response of the genetically encoded pH indicators is studied. The second Trp has been substituted by Ala and Glu to reduce self-quenching. Compared with the previously reported Trp-Trp-Ala-Ser (WWAS), the two new tetrapeptides, Trp-Ala-Ala-Ser (WAAS) and Trp-Glu-Ala-Ser (WEAS), have higher fluorescence quantum yields, longer fluorescence lifetimes, and more sensitive pH responses. As novel genetically encoded pH indicators, the N-terminal Trp-Ala and Trp-Glu could be fused to proteins for monitoring the environmental pH values during the studies of functional proteins. fluorescent sensor genetically encoded pH indicator Trp-Ala-Ala-Ser Trp-Glu-Ala-Ser Trp-Trp-Ala-Ser Cao, X. aut Zhou, Zh. aut Zhang, S. aut Pan, H. aut Chen, J. aut Xu, J. aut Enthalten in Journal of applied spectroscopy Springer US, 1966 84(2017), 4 vom: Sept., Seite 633-638 (DE-627)129972495 (DE-600)410515-1 (DE-576)015535800 0021-9037 nnns volume:84 year:2017 number:4 month:09 pages:633-638 https://doi.org/10.1007/s10812-017-0521-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 AR 84 2017 4 09 633-638 |
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10.1007/s10812-017-0521-4 doi (DE-627)OLC2034688082 (DE-He213)s10812-017-0521-4-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Li, L. verfasserin aut Fluorescence Dynamics of N-Terminal Tryptofan-X Residues in Polypeptide: pH Response 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC 2017 The influence of the second amino acid on the pH response of the genetically encoded pH indicators is studied. The second Trp has been substituted by Ala and Glu to reduce self-quenching. Compared with the previously reported Trp-Trp-Ala-Ser (WWAS), the two new tetrapeptides, Trp-Ala-Ala-Ser (WAAS) and Trp-Glu-Ala-Ser (WEAS), have higher fluorescence quantum yields, longer fluorescence lifetimes, and more sensitive pH responses. As novel genetically encoded pH indicators, the N-terminal Trp-Ala and Trp-Glu could be fused to proteins for monitoring the environmental pH values during the studies of functional proteins. fluorescent sensor genetically encoded pH indicator Trp-Ala-Ala-Ser Trp-Glu-Ala-Ser Trp-Trp-Ala-Ser Cao, X. aut Zhou, Zh. aut Zhang, S. aut Pan, H. aut Chen, J. aut Xu, J. aut Enthalten in Journal of applied spectroscopy Springer US, 1966 84(2017), 4 vom: Sept., Seite 633-638 (DE-627)129972495 (DE-600)410515-1 (DE-576)015535800 0021-9037 nnns volume:84 year:2017 number:4 month:09 pages:633-638 https://doi.org/10.1007/s10812-017-0521-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 AR 84 2017 4 09 633-638 |
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10.1007/s10812-017-0521-4 doi (DE-627)OLC2034688082 (DE-He213)s10812-017-0521-4-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Li, L. verfasserin aut Fluorescence Dynamics of N-Terminal Tryptofan-X Residues in Polypeptide: pH Response 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC 2017 The influence of the second amino acid on the pH response of the genetically encoded pH indicators is studied. The second Trp has been substituted by Ala and Glu to reduce self-quenching. Compared with the previously reported Trp-Trp-Ala-Ser (WWAS), the two new tetrapeptides, Trp-Ala-Ala-Ser (WAAS) and Trp-Glu-Ala-Ser (WEAS), have higher fluorescence quantum yields, longer fluorescence lifetimes, and more sensitive pH responses. As novel genetically encoded pH indicators, the N-terminal Trp-Ala and Trp-Glu could be fused to proteins for monitoring the environmental pH values during the studies of functional proteins. fluorescent sensor genetically encoded pH indicator Trp-Ala-Ala-Ser Trp-Glu-Ala-Ser Trp-Trp-Ala-Ser Cao, X. aut Zhou, Zh. aut Zhang, S. aut Pan, H. aut Chen, J. aut Xu, J. aut Enthalten in Journal of applied spectroscopy Springer US, 1966 84(2017), 4 vom: Sept., Seite 633-638 (DE-627)129972495 (DE-600)410515-1 (DE-576)015535800 0021-9037 nnns volume:84 year:2017 number:4 month:09 pages:633-638 https://doi.org/10.1007/s10812-017-0521-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 AR 84 2017 4 09 633-638 |
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Li, L. ddc 530 ssgn 11 misc fluorescent sensor misc genetically encoded pH indicator misc Trp-Ala-Ala-Ser misc Trp-Glu-Ala-Ser misc Trp-Trp-Ala-Ser Fluorescence Dynamics of N-Terminal Tryptofan-X Residues in Polypeptide: pH Response |
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Fluorescence Dynamics of N-Terminal Tryptofan-X Residues in Polypeptide: pH Response |
| abstract |
The influence of the second amino acid on the pH response of the genetically encoded pH indicators is studied. The second Trp has been substituted by Ala and Glu to reduce self-quenching. Compared with the previously reported Trp-Trp-Ala-Ser (WWAS), the two new tetrapeptides, Trp-Ala-Ala-Ser (WAAS) and Trp-Glu-Ala-Ser (WEAS), have higher fluorescence quantum yields, longer fluorescence lifetimes, and more sensitive pH responses. As novel genetically encoded pH indicators, the N-terminal Trp-Ala and Trp-Glu could be fused to proteins for monitoring the environmental pH values during the studies of functional proteins. © Springer Science+Business Media, LLC 2017 |
| abstractGer |
The influence of the second amino acid on the pH response of the genetically encoded pH indicators is studied. The second Trp has been substituted by Ala and Glu to reduce self-quenching. Compared with the previously reported Trp-Trp-Ala-Ser (WWAS), the two new tetrapeptides, Trp-Ala-Ala-Ser (WAAS) and Trp-Glu-Ala-Ser (WEAS), have higher fluorescence quantum yields, longer fluorescence lifetimes, and more sensitive pH responses. As novel genetically encoded pH indicators, the N-terminal Trp-Ala and Trp-Glu could be fused to proteins for monitoring the environmental pH values during the studies of functional proteins. © Springer Science+Business Media, LLC 2017 |
| abstract_unstemmed |
The influence of the second amino acid on the pH response of the genetically encoded pH indicators is studied. The second Trp has been substituted by Ala and Glu to reduce self-quenching. Compared with the previously reported Trp-Trp-Ala-Ser (WWAS), the two new tetrapeptides, Trp-Ala-Ala-Ser (WAAS) and Trp-Glu-Ala-Ser (WEAS), have higher fluorescence quantum yields, longer fluorescence lifetimes, and more sensitive pH responses. As novel genetically encoded pH indicators, the N-terminal Trp-Ala and Trp-Glu could be fused to proteins for monitoring the environmental pH values during the studies of functional proteins. © Springer Science+Business Media, LLC 2017 |
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Fluorescence Dynamics of N-Terminal Tryptofan-X Residues in Polypeptide: pH Response |
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Cao, X. Zhou, Zh Zhang, S. Pan, H. Chen, J. Xu, J. |
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Cao, X. Zhou, Zh Zhang, S. Pan, H. Chen, J. Xu, J. |
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129972495 |
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| doi_str |
10.1007/s10812-017-0521-4 |
| up_date |
2024-07-03T22:01:36.479Z |
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