ArticleJournal of the American Chemical Society2012
Two pyrenylalanines in dihydrofolate reductase form an excimer enabling the study of protein dynamics.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 35 citations in OpenAlex.
- Expanding the fluorescence toolkit: molecular design, synthesis and biological application of unnatural amino acids.Chemical science · 2025Review
- Facile synthesis of a novel genetically encodable fluorescent α-amino acid emitting greenish blue light.Chemical communications (Cambridge, England) · 2020Article
- Ligand-Dependent Conformational Dynamics of Dihydrofolate Reductase.Biochemistry · 2016Article
- Ribosome-Mediated Incorporation of Dipeptides and Dipeptide Analogues into Proteins in Vitro.Journal of the American Chemical Society · 2015Article
- Linking protein motion to enzyme catalysis.Molecules (Basel, Switzerland) · 2015Review
- Tryptophan-based fluorophores for studying protein conformational changes.Bioorganic & medicinal chemistry · 2014Article
- Extension and limits of the network of coupled motions correlated to hydride transfer in dihydrofolate reductase.Journal of the American Chemical Society · 2014Article
- Preservation of protein dynamics in dihydrofolate reductase evolution.The Journal of biological chemistry · 2013Article
- Fluorescent biphenyl derivatives of phenylalanine suitable for protein modification.Biochemistry · 2013Article
- Detection of dihydrofolate reductase conformational change by FRET using two fluorescent amino acids.Journal of the American Chemical Society · 2013Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Because of the lack of sensitivity to small changes in distance by available FRET pairs (a constraint imposed by the dimensions of the enzyme), a DHFR containing two pyrene moieties was prepared to enable the observation of excimer formation. Pyren-1-ylalanine was introduced into DHFR positions 16 and 49 using an in vitro expression system in the presence of pyren-1-ylalanyl-tRNA(CUA). Excimer formation (λ(ex) 342 nm; λ(em) 481 nm) was observed in the modified DHFR, which retained its catalytic competence and was studied under multiple and single turnover conditions. The excimer appeared to follow a protein conformational change after the H transfer involving the relative position and orientation of the pyrene moieties and is likely associated with product dissociation.
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Registered trials
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