FRET events in fluorescent pentapeptides containing aliphatic triazolo amino acid scaffolds: Role of spacer lengths
| Autor: | Subhendu Sekhar Bag, Afsana Yashmeen |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
chemistry.chemical_classification
Flexibility (anatomy) Stereochemistry General Chemical Engineering General Physics and Astronomy Peptide 02 engineering and technology General Chemistry 010402 general chemistry 021001 nanoscience & nanotechnology 01 natural sciences Acceptor Pentapeptide repeat Fluorescence 0104 chemical sciences Amino acid Förster resonance energy transfer medicine.anatomical_structure chemistry medicine 0210 nano-technology |
| Zdroj: | Journal of Photochemistry and Photobiology A: Chemistry. 378:171-183 |
| ISSN: | 1010-6030 |
| DOI: | 10.1016/j.jphotochem.2019.04.024 |
| Popis: | The FRET efficiencies in donor/acceptor pairs in the two termini of designed fluorescent pentapeptides depend on the flexibility of two arms of triazolyl amino acid scaffolds positioned in the center of the backbones inducing predominant β-sheet conformations. Flexible N-Terminus of the scaffold in a pentapeptide has led to higher FRET efficiency and makes it different from other peptide with flexible C-terminus. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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