Abstract
Frequency-domain fluorescence spectroscopy was employed to examine the decays of tryptophan in Boc-Trp-Met-Asp-Phe-NH2 (donor) and {A figure is presented} (donor-acceptor pair). The efficiency of energy transfer in the thiopeptide amounted to 60% The measured dispersion of fluorescence decay times was used to recover the donor-acceptor distance distribution. The parameters of the Gaussian distance distribution obtained for this peptide (r, the mean distance (9 Å); hw, the halfwidth (25 Å)) indicate the lack of a distinct favorable conformation.
Original language | English |
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Pages (from-to) | 43-49 |
Number of pages | 7 |
Journal | Biophysical Chemistry |
Volume | 32 |
Issue number | 1 |
DOIs | |
State | Published - Oct 1988 |
Keywords
- Distance distribution
- Energy transfer
- Fluorescence spectroscopy
- Frequency-domain fluorometry
- Thiopeptide