ArticleBiochemistry2008
Using an amino acid fluorescence resonance energy transfer pair to probe protein unfolding: application to the villin headpiece subdomain and the LysM domain.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 63 citations in OpenAlex.
- Pathfinder: Protein folding pathway prediction based on conformational sampling.PLoS computational biology · 2023Article
- Article
- Unraveling Complex Local Protein Environments with 4-Cyano-l-phenylalanine.The journal of physical chemistry. B · 2022Article
- Fast label-free identification of bacteria by synchronous fluorescence of amino acids.Analytical and bioanalytical chemistry · 2021Article
- Vibrational Approach to the Dynamics and Structure of Protein Amyloids.Molecules (Basel, Switzerland) · 2019Review
- Heterogeneity in the Folding of Villin Headpiece Subdomain HP36.The journal of physical chemistry. B · 2018Article
- Residue-Specific Dynamics and Local Environmental Changes in Aβ40 Oligomer and Fibril Formation.Angewandte Chemie (International ed. in English) · 2018Article
- Exploring local solvation environments of a heme protein using the spectroscopic reporter 4-cyano-l-phenylalanine.RSC advances · 2018Article
- Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein.Biophysical journal · 2018Article
- Selenomethionine, p-cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure.Chemical communications (Cambridge, England) · 2016Article
- Probing the effectiveness of spectroscopic reporter unnatural amino acids: a structural study.Acta crystallographica. Section D, Structural biology · 2016Article
- Sensing pH via p-cyanophenylalanine fluorescence: Application to determine peptide pKa and membrane penetration kinetics.Analytical biochemistry · 2015Article
- p-Cyanophenylalanine and selenomethionine constitute a useful fluorophore-quencher pair for short distance measurements: application to polyproline peptides.Physical chemistry chemical physics : PCCP · 2015Article
- Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications.Applied microbiology and biotechnology · 2014Review
- Sensitive, site-specific, and stable vibrational probe of local protein environments: 4-azidomethyl-L-phenylalanine.The journal of physical chemistry. B · 2013Article
- Quenching ofChemical physics letters · 2013Article
- Fast dynamics of HP35 for folded and urea-unfolded conditions.The journal of physical chemistry. B · 2012Article
- Native state conformational heterogeneity of HP35 revealed by time-resolved FRET.The journal of physical chemistry. B · 2012Article
- Conformational dynamics and stability of HP35 studied with 2D IR vibrational echoes.Journal of the American Chemical Society · 2012Article
- Minimalist probes for studying protein dynamics: thioamide quenching of selectively excitable fluorescent amino acids.Journal of the American Chemical Society · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Previously, we have shown that p-cyanophenylalanine (Phe CN) and tryptophan (Trp) constitute an efficient fluorescence resonance energy transfer (FRET) pair that has several advantages over commonly used dye pairs. Here, we aim to examine the general applicability of this FRET pair in protein folding-unfolding studies by applying it to the urea-induced unfolding transitions of two small proteins, the villin headpiece subdomain (HP35) and the lysin motif (LysM) domain. Depending on whether Phe CN is exposed to solvent, we are able to extract either qualitative information about the folding pathway, as demonstrated by HP35, which has been suggested to unfold in a stepwise manner, or quantitative thermodynamic and structural information, as demonstrated by LysM, which has been shown to be an ideal two-state folder. Our results show that the unfolding transition of HP35 reported by FRET occurs at a denaturant concentration lower than that measured by circular dichroism (CD) and that the loop linking helix 2 and helix 3 remains compact in the denatured state, which are consistent with the notion that HP35 unfolds in discrete steps and that its unfolded state contains residual structures. On the other hand, our FRET results on the LysM domain allow us to develop a model for extracting structural and thermodynamic parameters about its unfolding, and we find that our results are in agreement with those obtained by other methods. Given the fact that Phe CN is a non-natural amino acid and, thus, amenable to incorporation into peptides and proteins via existing peptide synthesis and protein expression methods, we believe that the FRET method demonstrated here is widely applicable to protein conformational studies, especially to the study of relatively small proteins.
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