Time-Resolved Fluorescence and 1H NMR Studies of Tyrosyl Residues in Oxytocin and Small Peptides: Correlation of NMR-Determined Conformations of Tyrosyl Residues and Fluorescence Decay Kinetics

J. B. Alexander Ross, Angeliki Buku, Herman R. Wyssbrod, William R. Laws, John C. Sutherland

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Steady-state and time-resolved fluorescence properties of the single tyrosyl residue in oxytocin and two oxytocin derivatives at pH 3 are presented. The decay kinetics of the tyrosyl residue are complex for each compound. By use of a linked-function analysis, the fluorescence kinetics can be explained by a ground-state rotamer model. The linked function assumes that the preexponential weighting factors (amplitudes) of the fluorescence decay constants have the same relative relationship as the 1H NMR determined phenol side-chain rotamer populations. According to this model, the static quenching of the oxytocin fluorescence can be attributed to an interaction between one specific rotamer population of the tyrosine ring and the internal disulfide bridge.

Original languageEnglish (US)
Pages (from-to)607-612
Number of pages6
JournalBiochemistry
Volume25
Issue number3
DOIs
StatePublished - Jan 1 1986

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Oxytocin
Conformations
Fluorescence
Nuclear magnetic resonance
Peptides
Kinetics
Phenol
Disulfides
Ground state
Population
Tyrosine
Quenching
Derivatives
Proton Magnetic Resonance Spectroscopy

ASJC Scopus subject areas

  • Biochemistry

Cite this

Time-Resolved Fluorescence and 1H NMR Studies of Tyrosyl Residues in Oxytocin and Small Peptides : Correlation of NMR-Determined Conformations of Tyrosyl Residues and Fluorescence Decay Kinetics. / Alexander Ross, J. B.; Buku, Angeliki; Wyssbrod, Herman R.; Laws, William R.; Sutherland, John C.

In: Biochemistry, Vol. 25, No. 3, 01.01.1986, p. 607-612.

Research output: Contribution to journalArticle

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abstract = "Steady-state and time-resolved fluorescence properties of the single tyrosyl residue in oxytocin and two oxytocin derivatives at pH 3 are presented. The decay kinetics of the tyrosyl residue are complex for each compound. By use of a linked-function analysis, the fluorescence kinetics can be explained by a ground-state rotamer model. The linked function assumes that the preexponential weighting factors (amplitudes) of the fluorescence decay constants have the same relative relationship as the 1H NMR determined phenol side-chain rotamer populations. According to this model, the static quenching of the oxytocin fluorescence can be attributed to an interaction between one specific rotamer population of the tyrosine ring and the internal disulfide bridge.",
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AB - Steady-state and time-resolved fluorescence properties of the single tyrosyl residue in oxytocin and two oxytocin derivatives at pH 3 are presented. The decay kinetics of the tyrosyl residue are complex for each compound. By use of a linked-function analysis, the fluorescence kinetics can be explained by a ground-state rotamer model. The linked function assumes that the preexponential weighting factors (amplitudes) of the fluorescence decay constants have the same relative relationship as the 1H NMR determined phenol side-chain rotamer populations. According to this model, the static quenching of the oxytocin fluorescence can be attributed to an interaction between one specific rotamer population of the tyrosine ring and the internal disulfide bridge.

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