title: Distribution of distances in thiopeptides by fluorescence energy transfer and frequency-domain fluorometry.
abstract: Frequency-domain fluorescence spectroscopy was employed to examine the decays of tryptophan in Boc-Trp-Met-Asp-Phe-NH2 (donor) and (Formula: see text) (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 A); hw, the halfwidth (25 A)) indicate the lack of a distinct favorable conformation.
authors.affiliation: University of Maryland, School of Medicine, Department of Biological Chemistry, Baltimore 21201.
authors.forename: W M
authors.initials: WM
authors.lastname: Wiczk
authors.forename: I
authors.initials: I
authors.lastname: Gryczynski
authors.forename: H
authors.initials: H
authors.lastname: Szmacinski
authors.forename: M L
authors.initials: ML
authors.lastname: Johnson
authors.forename: M
authors.initials: M
authors.lastname: Kruszynski
authors.forename: J
authors.initials: J
authors.lastname: Zboinska
mesh_terms: D004735:Energy Transfer; D010418:Pentagastrin / Q000031:analogs & derivatives* / Q000138:chemical synthesis; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence / Q000379:methods; D013438:Sulfhydryl Compounds / Q000138:chemical synthesis; D014364:Tryptophan
chemical_list: D013438:Sulfhydryl Compounds; C041024:tertiary-butyloxycarbonyl-glycyl-tryptophyl-methionyl-aspartyl-phenylalaninamide; D014364:Tryptophan; D010418:Pentagastrin