Distribution of distances in thiopeptides by fluorescence energy transfer and frequency-domain fluorometry

Wieslaw M. Wiczk; Ignacy Gryczynski; Henryk Szmacinski; Michael L. Johnson; Marian Kruszynski; Jolanta Zboinska

doi:10.1016/0301-4622(88)85032-4

Distribution of distances in thiopeptides by fluorescence energy transfer and frequency-domain fluorometry

Wieslaw M. Wiczk, Ignacy Gryczynski, Henryk Szmacinski, Michael L. Johnson, Marian Kruszynski, Jolanta Zboinska

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

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
Pages (from-to)	43-49
Number of pages	7
Journal	Biophysical Chemistry
Volume	32
Issue number	1
DOIs	https://doi.org/10.1016/0301-4622(88)85032-4
State	Published - Oct 1988

Keywords

Distance distribution
Energy transfer
Fluorescence spectroscopy
Frequency-domain fluorometry
Thiopeptide

Access to Document

10.1016/0301-4622(88)85032-4

Cite this

@article{0b2aac1c77634668bcbc8bbec51adfed,

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 {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 {\AA}); hw, the halfwidth (25 {\AA})) indicate the lack of a distinct favorable conformation.",

keywords = "Distance distribution, Energy transfer, Fluorescence spectroscopy, Frequency-domain fluorometry, Thiopeptide",

author = "Wiczk, {Wieslaw M.} and Ignacy Gryczynski and Henryk Szmacinski and Johnson, {Michael L.} and Marian Kruszynski and Jolanta Zboinska",

note = "Funding Information: This work was supported by grants GM-35154 from the National Institutes of Health, DMB-8511065 for frequency-domain instrumentation for the National Science Foundation and a grant C.P.B.R.-3.8.5. from the Polish Academy of Science.",

year = "1988",

month = oct,

doi = "10.1016/0301-4622(88)85032-4",

language = "English",

volume = "32",

pages = "43--49",

journal = "Biophysical Chemistry",

issn = "0301-4622",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

T1 - Distribution of distances in thiopeptides by fluorescence energy transfer and frequency-domain fluorometry

AU - Wiczk, Wieslaw M.

AU - Gryczynski, Ignacy

AU - Szmacinski, Henryk

AU - Johnson, Michael L.

AU - Kruszynski, Marian

AU - Zboinska, Jolanta

N1 - Funding Information: This work was supported by grants GM-35154 from the National Institutes of Health, DMB-8511065 for frequency-domain instrumentation for the National Science Foundation and a grant C.P.B.R.-3.8.5. from the Polish Academy of Science.

PY - 1988/10

Y1 - 1988/10

N2 - 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.

AB - 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.

KW - Distance distribution

KW - Energy transfer

KW - Fluorescence spectroscopy

KW - Frequency-domain fluorometry

KW - Thiopeptide

UR - http://www.scopus.com/inward/record.url?scp=0024100874&partnerID=8YFLogxK

U2 - 10.1016/0301-4622(88)85032-4

DO - 10.1016/0301-4622(88)85032-4

M3 - Article

C2 - 3233313

AN - SCOPUS:0024100874

SN - 0301-4622

VL - 32

SP - 43

EP - 49

JO - Biophysical Chemistry

JF - Biophysical Chemistry

IS - 1

ER -

Distribution of distances in thiopeptides by fluorescence energy transfer and frequency-domain fluorometry

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this