Fluorescence Sensor Peptide for Protein Kinase Activity.
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Accession number;04A0258626
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| Title;Fluorescence Sensor Peptide for Protein Kinase Activity. |
| Author;
YOKOYAMA KENJI
(National Inst. Advanced Industrial Sci. and Technol., JPN)
INOUE OSAMU
(Japan Advanced Inst. Sci. and Technol., Hokuriku)
IKEDA KENJIRO
(Japan Advanced Inst. Sci. and Technol., Hokuriku)
MORITA YASUTAKA
(Japan Advanced Inst. Sci. and Technol., Hokuriku)
TAMIYA EIICHI
(Japan Advanced Inst. Sci. and Technol., Hokuriku)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.18th;NO.;PAGE.88-89(2003)
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| Figure&Table&Reference;FIG.2 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;In this work, we synthesized decamer and 15mer peptides, which include amino acid sequence of phosphorylated site of protein kinase A (PKA). Ser is phosphorylated by PKA in the cell. EDANS-modified decamer and 15mer peptides, GLRRASLGE(EDANS)G, and GDENLRRASLGEDE(EDANS)G, were synthesized on bead. After cleavage, dabcyl group was attached at the N-terminal .ALPHA.-amino group. Ser-phosphorylated sensor peptides were also synthesized. Fluorescence property of the peptides modified with EDANS and dabcyl was investigated. Energy transfer from EDANS to DABCYL, quenching by DABCYL, was reduced by phosphorylation of Ser. Peptide main chain was stretched by increase in hydrophilicity, and the distance between the fluorescent dye and quencher increased. Since distance between EDANS and dabcyl of the 15mer peptide is longer than 10mer peptide, 15mer peptide demonstrated the greater fluorescence intensity. (author abst.) |
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