ArticleScientific reports2020
What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 51 citations in OpenAlex.
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- Engineered Proteins and Materials Utilizing Residue-Specific Noncanonical Amino Acid Incorporation.Chemical reviews · 2024Review
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- Upstream of N-Ras C-terminal cold shock domains mediate poly(A) specificity in a novel RNA recognition mode and bind poly(A) binding protein.Nucleic acids research · 2023Article
- Fluorinated Protein and Peptide Materials for Biomedical Applications.Pharmaceuticals (Basel, Switzerland) · 2022Review
- The Magic of Linking Rings: Discovery of a Unique Photoinduced Fluorescent Protein Crosslink.Journal of the American Chemical Society · 2022Article
- Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy.International journal of molecular sciences · 2022Article
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- Development and Validation of Fluorinated, Aromatic Amino Acid Parameters for Use with the AMBER ff15ipq Protein Force Field.The journal of physical chemistry. A · 2022Article
- Fluorine-Containing Drug Administration in Rats Results in Fluorination of Selected Proteins in Liver and Brain Tissue.International journal of molecular sciences · 2022Article
- Small, but powerful and attractive:Structure (London, England : 1993) · 2022Review
- Natural and Synthetic Halogenated Amino Acids-Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics.Molecules (Basel, Switzerland) · 2021Review
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Authors and funding
5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Fluorine labelling represents one promising approach to study proteins in their native environment due to efficient suppressing of background signals. Here, we systematically probe inherent thermodynamic and structural characteristics of the Cold shock protein B from Bacillus subtilis (BsCspB) upon fluorine labelling. A sophisticated combination of fluorescence and NMR experiments has been applied to elucidate potential perturbations due to insertion of fluorine into the protein. We show that single fluorine labelling of phenylalanine or tryptophan residues has neither significant impact on thermodynamic stability nor on folding kinetics compared to wild type BsCspB. Structure determination of fluorinated phenylalanine and tryptophan labelled BsCspB using X-ray crystallography reveals no displacements even for the orientation of fluorinated aromatic side chains in comparison to wild type BsCspB. Hence we propose that single fluorinated phenylalanine and tryptophan residues used for protein labelling may serve as ideal probes to reliably characterize inherent features of proteins that are present in a highly biological context like the cell.
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