ArticleProceedings of the National Academy of Sciences of the United States of America2001
Solution 19F nuclear Overhauser effects in structural studies of the cytoplasmic domain of mammalian rhodopsin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 86 citations in OpenAlex.
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- Enlarging the scenario of site directedScientific reports · 2023Article
- Interdisciplinary biophysical studies of membrane proteins bacteriorhodopsin and rhodopsin.Biophysical reviews · 2023Review
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- G Protein-coupled Receptor (GPCR) Reconstitution and Labeling for Solution Nuclear Magnetic Resonance (NMR) Studies of the Structural Basis of Transmembrane Signaling.Molecules (Basel, Switzerland) · 2022Review
- 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
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- Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics.Magnetic resonance (Gottingen, Germany) · 2021Review
- Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020Review
- Solution NMR spectroscopy of GPCRs: Residue-specific labeling strategies with a focus onMethods in cell biology · 2019Article
- Evaluating electronic structure methods for accurate calculation ofJournal of computational chemistry · 2017Article
- In-Membrane Chemical Modification (IMCM) for Site-Specific Chromophore Labeling of GPCRs.Angewandte Chemie (International ed. in English) · 2015Article
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- Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.Biochemistry · 2014Article
- Chemical modifications of respiratory complex I for structural and functional studies.Journal of bioenergetics and biomembranes · 2014Review
- β₂-adrenergic receptor activation by agonists studied with ¹⁹F NMR spectroscopy.Angewandte Chemie (International ed. in English) · 2013Article
- Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs.Current opinion in structural biology · 2013Review
- Stabilization of the single-chain fragment variable by an interdomain disulfide bond and its effect on antibody affinity.International journal of molecular sciences · 2010Article
- What site-directed labeling studies tell us about the mechanism of rhodopsin activation and G-protein binding.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2010Review
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6 authors at 1 institution in 1 country.
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Abstract
19F nuclear Overhauser effects (NOEs) between fluorine labels on the cytoplasmic domain of rhodopsin solubilized in detergent micelles are reported. Previously, high-resolution solution (19)F NMR spectra of fluorine-labeled rhodopsin in detergent micelles were described, demonstrating the applicability of this technique to studies of tertiary structure in the cytoplasmic domain. To quantitate tertiary contacts we have applied a transient one-dimensional difference NOE solution (19)F NMR experiment to this system, permitting assessment of proximities between fluorine labels specifically incorporated into different regions of the cytoplasmic face. Three dicysteine substitution mutants (Cys-140-Cys-316, Cys-65-Cys-316, and Cys-139-Cys-251) were labeled by attachment of the trifluoroethylthio group through a disulfide linkage. Each mutant rhodopsin was prepared (8-10 mg) in dodecylmaltoside and analyzed at 20 degrees C by solution (19)F NMR. Distinct chemical shifts were observed for all of the rhodopsin (19)F labels in the dark. An up-field shift of the Cys-316 resonance in the Cys-65-Cys-316 mutant suggests a close proximity between the two residues. When analyzed for (19)F-(19)F NOEs, a moderate negative enhancement was observed for the Cys-65-Cys-316 pair and a strong negative enhancement was observed for the Cys-139-Cys-251 pair, indicating proximity between these sites. No NOE enhancement was observed for the Cys-140-Cys-316 pair. These NOE effects demonstrate a solution (19)F NMR method for analysis of tertiary contacts in high molecular weight proteins, including membrane proteins.
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