ArticleJournal of fluorescence2009
Fluorescence lifetimes of tryptophan: structural origin and relation with So --> 1Lb and So --> 1La transitions.
Article in Journal of fluorescence, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Protein-Mediated Bimetallic Nanoclusters: Effect of Protein Nature on Structure, Optical Property and Cytotoxicity.Nanomaterials (Basel, Switzerland) · 2026Article
- Selective Excitation of theACS omega · 2024Article
- Time-Resolved Fluorescence Spectroscopy of Blood, Plasma and Albumin as a Potential Diagnostic Tool for Acute Inflammation in COVID-19 Pneumonia Patients.International journal of molecular sciences · 2023Article
- A study of the oxidative processes in human plasma by time-resolved fluorescence spectroscopy.Scientific reports · 2022Article
- Exploring protein solution structure: Second moments of fluorescent spectra report heterogeneity of tryptophan rotamers.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2015Article
- Origin of tryptophan fluorescence lifetimes. Part 2: fluorescence lifetimes origin of tryptophan in proteins.Journal of fluorescence · 2014Article
- Origin of tryptophan fluorescence lifetimes part 1. Fluorescence lifetimes origin of tryptophan free in solution.Journal of fluorescence · 2014Article
- Do hydration dynamics follow the structural perturbation during thermal denaturation of a protein: a terahertz absorption study.Biophysical journal · 2011Article
- Sub-structures formed in the excited state are responsible for tryptophan residues fluorescence in β-lactoglobulin.Journal of fluorescence · 2011Article
- Relation between proteins tertiary structure, tryptophan fluorescence lifetimes and tryptophan S(o)→(1)L(b) and S(o)→(1)L(a) transitions. Studies on α1-acid glycoprotein and β-lactoglobulin.Journal of fluorescence · 2011Article
- Effect of 1-aminoanthracene (1-AMA) binding on the structure of three lipocalin proteins, the dimeric β lactoglobulin, the dimeric odorant binding protein and the monomeric α1-acid glycoprotein. Fluorescence spectra and lifetimes studies.Journal of fluorescence · 2010Article
- Origin of fluorescence lifetimes in human serum albumin. Studies on native and denatured protein.Journal of fluorescence · 2010Article
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Authors and funding
1 author.
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Abstract
We measured fluorescence lifetimes of L-Tryptophan dissolved in de-ionized water and in ethanol in the absence and the presence of high progesterone concentrations. The hormone absorbs between 220 and 280 with a peak around 250 nm, while its absorption is equal to zero beyond 280 nm. Tryptophan excitation spectrum recorded in presence of progesterone shows that the S(o) --> 1L(a) transition is completely abolished while the S(o) --> 1L(b) transition is not affected. Emission of L-tryptophan in water occurs with two fluorescence lifetimes, 0.40 and 2.8 ns. In ethanol, three fluorescence lifetimes equal to around 0.2, 1.8 and 4.8 ns were observed. Addition of progesterone to the medium does not affect any of the fluorescence lifetimes indicating clearly that both transitions could induce tryptophan excitation and that recorded fluorescence lifetimes could be assigned to sub-structures generated in the excited state.
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