ArticleJournal of fluorescence2014
Origin of tryptophan fluorescence lifetimes part 1. Fluorescence lifetimes origin of tryptophan free in solution.
Article in Journal of fluorescence, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 53 citations in OpenAlex.
- Spectroscopic and Pulse Radiolysis Studies of Water-Ethanolic Solutions of Albumins: Insight into Serum Albumin Aggregation.International journal of molecular sciences · 2025Article
- Time-resolved fluorescence of tryptophan characterizes membrane perturbation by cyclic lipopeptides.Biophysical journal · 2024Article
- Electronic Energy Migration in Microtubules.ACS central science · 2023Article
- Evaluation of the Antiproliferative Properties of CpRu Complexes Containing N-Methylated Triazaphosphaadamantane Derivatives.Bioinorganic chemistry and applications · 2023Article
- How Do Phenolic Acids Change the Secondary and Tertiary Structure of Gliadin? Studies with an Application of Spectroscopic Techniques.International journal of molecular sciences · 2022Article
- Probing of carotenoid-tryptophan hydrogen bonding dynamics in the single-tryptophan photoactive Orange Carotenoid Protein.Scientific reports · 2020Article
- Tryptophan / Dextran70 Based - Fluorescent Silver Nanoparticles: Synthesis and Physicochemical Properties.Journal of fluorescence · 2019Article
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- Experimental approach to study the effect of mutations on the protein folding pathway.PloS one · 2019Article
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- Utility of 5-Cyanotryptophan Fluorescence as a Sensitive Probe of Protein Hydration.The journal of physical chemistry. B · 2016Article
- Exploring protein solution structure: Second moments of fluorescent spectra report heterogeneity of tryptophan rotamers.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2015Article
- Intrinsic tryptophan fluorescence in the detection and analysis of proteins: a focus on Förster resonance energy transfer techniques.International journal of molecular sciences · 2014Review
- Native Fluorescence and Time Resolved Fluorescence Spectroscopic Characterization of Normal and Malignant Oral Tissues Under UV Excitation--an In Vitro Study.Journal of fluorescence · 2014Article
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Authors and funding
1 author at 1 institution in 1 country.
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Abstract
Fluorescence intensity decays of L-tryptophan free in polar, hydrophobic and mixture of polar-hydrophobic solvents were recorded along the emission spectrum (310-410 nm). Analysis of the data show that emission of tryptophan occurs with two lifetimes in 100% polar and hydrophobic environments. The values of the two lifetimes are not the same in both environments while their populations (pre-exponentials values) are identical. Fluorescence lifetimes and pre-exponentials values do not change with the excitation wavelength and thus are independent of excitation energy. Our results indicate that tryptophan emission occurs from two specific sub-structures existing in the excited state. These sub-structures differ from those present in the ground states and characterize an internal property and/or organization of the tryptophan structure in the excited state. By sub-substructure, we mean here tryptophan backbone and its electronic cloud. In ethanol, three fluorescence lifetimes were measured; two lifetimes are very close to those observed in water (0.4-0.5 ns and 2-4 ns). Presence of a third lifetime for tryptophan in ethanol results from the interaction of both hydrophobic and hydrophilic dipoles or chemical functions of ethanol with the fluorophore.
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