Ultrafast polarized fluorescence measurements on monomeric and self-associated melittin
| العنوان: | Ultrafast polarized fluorescence measurements on monomeric and self-associated melittin |
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| المؤلفون: | O.F.A. Larsen, H. van Amerongen, I.H.M. van Stokkum, Ruud Kraayenhof, Anjali Pandit, R. van Grondelle |
| المساهمون: | Structural Biology, BioAnalytical Chemistry, Physical Computer Science, Biophysics Photosynthesis/Energy |
| المصدر: | Pandit, A, Larsen, O F A, van Stokkum, I H M, van Grondelle, R, Kraayenhof, R & van Amerongen, H 2003, ' Ultrafast polarized fluorescence measurements on monomeric and self-associated melittin ', Journal of Physical Chemistry B, vol. 107, pp. 3086-3090 . https://doi.org/10.1021/jp021757a Journal of Physical Chemistry B, 107, 3086-3090. American Chemical Society The Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 107, 3086-3090 Journal of Physical Chemistry B, 107(13), 3086-3090. American Chemical Society Pandit, A, Larsen, O F A, van Stokkum, I H M, van Grondelle, R, Kraayenhof, R & van Amerongen, H 2003, ' Ultrafast polarized fluorescence measurements on monomeric and self-associated melittin ', Journal of Physical Chemistry B, vol. 107, no. 13, pp. 3086-3090 . https://doi.org/10.1021/jp021757a The Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical 107 (2003) |
| بيانات النشر: | American Chemical Society, 2003. |
| سنة النشر: | 2003 |
| مصطلحات موضوعية: | conformational dynamics, Analytical chemistry, Biophysics, anisotropy, Melittin, Spectral line, decay, chemistry.chemical_compound, energy-transfer, Materials Chemistry, refinement, tryptophan, Physical and Theoretical Chemistry, Anisotropy, parameters, Streak camera, excitation, secondary structure, Fluorescence, Surfaces, Coatings and Films, Biofysica, chemistry, Distilled water, Picosecond, protein, SDG 6 - Clean Water and Sanitation, Fluorescence anisotropy |
| الوصف: | The anisotropic and magic-angle fluorescence decay of the single tryptophan (Trp) residue of melittin, a bee venom peptide, was investigated by time-resolved fluorescence anisotropy using a streak camera setup. The peptide was dissolved either in distilled water or in Hepes/NaOH buffer containing low (10 mM) or high (2 M) concentrations of NaCl, the latter resulting in tetramerized melittin. For melittin in distilled water and low NaCl concentration, two anisotropy decay times were found in the order of similar to50 and similar to800 picoseconds, reflecting, local and overall peptide dynamics, respectively, and for tetramerized melittin, two anisotropy decay times of similar to200 and similar to5500 picoseconds were found. Decay-associated spectra of the isotropic fluorescence decay show three time components in the range of similar to20 picoseconds, similar to500 picoseconds, and similar to3500 picoseconds, respectively. The relative amplitudes of the latter two change upon the self-association of melittin. This change can be explained by the existence of different rotamers of Trp in melittin, of which one is more favored in the melittin tetramer than in the melittin monomer. |
| وصف الملف: | application/pdf; application/octet-stream |
| اللغة: | English |
| تدمد: | 1520-5207 1520-6106 3086-3090 |
| DOI: | 10.1021/jp021757a |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2a077c7e90140dcc6d36283dbff1246 https://hdl.handle.net/1871/38663 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....a2a077c7e90140dcc6d36283dbff1246 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15205207 15206106 30863090 |
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| DOI: | 10.1021/jp021757a |