Ultrafast polarized fluorescence measurements on Tryptophan and a Tryptophan-containing peptide
| Autor: | I.H.M. van Stokkum, Anjali Pandit, R. van Grondelle, O.F.A. Larsen, H. van Amerongen |
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| Přispěvatelé: | BioAnalytical Chemistry, Biophysics Photosynthesis/Energy |
| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
spectroscopy
conformational dynamics Biophysics Peptide Photochemistry decay Nuclear magnetic resonance alpha-helix depolarization SDG 3 - Good Health and Well-being excited-state Materials Chemistry rna Physical and Theoretical Chemistry hiv-1 rev Spectroscopy Conformational isomerism Indole test chemistry.chemical_classification Chemistry Tryptophan Fluorescence proteins Surfaces Coatings and Films Biofysica indole Picosecond Fluorescence anisotropy |
| Zdroj: | Larsen, O F A, van Stokkum, I H M, Pandit, A, van Grondelle, R & van Amerongen, H 2003, ' Ultrafast polarized fluorescence measurements on tryptophan and a tryptophan-containing peptide ', Journal of Physical Chemistry B, vol. 107, no. 13, pp. 3080-3085 . https://doi.org/10.1021/jp021756i The Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 107, 3080-3085 Journal of Physical Chemistry B, 107(13), 3080-3085. American Chemical Society The Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical 107 (2003) |
| ISSN: | 1520-6106 |
| DOI: | 10.1021/jp021756i |
| Popis: | In this work polarized picosecond fluorescence measurements were performed on isolated tryptophan and tryptophan in a small 22-mer peptide using a streak camera coupled to a spectrograph as a detection system. In both cases the fluorescence decay was multiexponential with decay times of similar to500 ps, and similar to4 ns. Surprisingly, also a short-lived (similar to16 ps) isotropic fluorescence component was found for both tryptophan and the peptide which, to our knowledge. has never been observed before. Fluorescence anisotropy data showed rotational correlation times of 155 ps and 1.5 ns for the peptide, reflecting local and overall peptide dynamics, respectively. Recently it was argued [Lakowicz. J. R. Photochem. Photobiol. 2000, 72, 421] that the nonexponential fluorescence decay of tryptophan in proteins is mainly due to spectral relaxation, whereas for isolated tryptophan it is due to different rotamers. Our results do not support this view. In contrast we conclude in both cases that the different fluorescence decay times should be ascribed to different rotameric states. |
| Databáze: | OpenAIRE |
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