ArticleProtein science : a publication of the Protein Society2017
The fluorescence intensities ratio is not a reliable parameter for evaluation of protein unfolding transitions.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed.
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- Evaluation of the Functional Properties and Edible Safety of Concocted Xanthii Fructus Protein.Foods (Basel, Switzerland) · 2025Article
- pH modulates efficiency of singlet oxygen production by flavin cofactors.RSC advances · 2024Article
- Salt-Specific Suppression of the Cold Denaturation of Thermophilic Multidomain Initiation Factor 2.International journal of molecular sciences · 2023Article
- Widespread amyloidogenicity potential of multiple myeloma patient-derived immunoglobulin light chains.BMC biology · 2023Article
- Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores.STAR protocols · 2022Article
- eSPC: an online data-analysis platform for molecular biophysics.Acta crystallographica. Section D, Structural biology · 2021Article
- Stabilization Effect of Intrinsically Disordered Regions on Multidomain Proteins: The Case of the Methyl-CpG Protein 2, MeCP2.Biomolecules · 2021Article
- FoldAffinity: binding affinities from nDSF experiments.Scientific reports · 2021Article
- Assessing and Improving Protein Sample Quality.Methods in molecular biology (Clifton, N.J.) · 2021Article
- A kinetic coupling between protein unfolding and aggregation controls time-dependent solubility of the human myeloma antibody light chain.Protein science : a publication of the Protein Society · 2020Article
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- The structural basis of nanobody unfolding reversibility and thermoresistance.Scientific reports · 2018Article
- Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.International journal of molecular sciences · 2018Article
- Article
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Abstract
Monitoring the fluorescence of proteins, particularly the fluorescence of intrinsic tryptophan residues, is a popular method often used in the analysis of unfolding transitions (induced by temperature, chemical denaturant, and pH) in proteins. The tryptophan fluorescence provides several suitable parameters, such as steady-state fluorescence intensity, apparent quantum yield, mean fluorescence lifetime, position of emission maximum that are often utilized for the observation of the conformational/unfolding transitions of proteins. In addition, the fluorescence intensities ratio at different wavelengths (usually at 330 nm and 350 nm) is becoming an increasingly popular parameter for the evaluation of thermal transitions. We show that, under certain conditions, the use of this parameter for the analysis of unfolding transitions leads to the incorrect determination of thermodynamic parameters characterizing unfolding transitions in proteins (e.g., melting temperature) and, hence, can compromise the hit identification during high-throughput drug screening campaigns.
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