ArticleJournal of biomolecular NMR2007
Combined solid state and solution NMR studies of alpha,epsilon-15N labeled bovine rhodopsin.
Article in Journal of biomolecular NMR, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Gobind's last graduate student.Biophysical reviews · 2023Article
- Magic angle spinning NMR of G protein-coupled receptors.Progress in nuclear magnetic resonance spectroscopy · 2022Review
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Light Dynamics of the Retinal-Disease-Relevant G90D Bovine Rhodopsin Mutant.Angewandte Chemie (International ed. in English) · 2020Article
- Influence of Arrestin on the Photodecay of Bovine Rhodopsin.Angewandte Chemie (International ed. in English) · 2015Article
- Large-scale production and protein engineering of G protein-coupled receptors for structural studies.Frontiers in pharmacology · 2015Review
- Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.Biochemistry · 2014Article
- Amino acid conservation and interactions in rhodopsin: probing receptor activation by NMR spectroscopy.Biochimica et biophysica acta · 2014Review
- Isotope labeling in mammalian cells.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.Biochimica et biophysica acta · 2011Article
- Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.Journal of biomolecular NMR · 2011Article
- Structure and function of G protein-coupled receptors using NMR spectroscopy.Progress in nuclear magnetic resonance spectroscopy · 2010Review
- Preparation of stable isotope-labeled peripheral cannabinoid receptor CB2 by bacterial fermentation.Protein expression and purification · 2010Article
- Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Perspectives on NMR in drug discovery: a technique comes of age.Nature reviews. Drug discovery · 2008Review
- Isotope labeling of mammalian GPCRs in HEK293 cells and characterization of the C-terminus of bovine rhodopsin by high resolution liquid NMR spectroscopy.Journal of biomolecular NMR · 2008Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rhodopsin is the visual pigment of the vertebrate rod photoreceptor cell and is the only member of the G protein coupled receptor family for which a crystal structure is available. Towards the study of dynamics in rhodopsin, we report NMR-spectroscopic investigations of alpha,epsilon-15N-tryptophan labeled rhodopsin in detergent micelles and reconstituted in phospholipids. Using a combination of solid state 13C,15N-REDOR and HETCOR experiments of all possible 13C'(i-1) carbonyl/15N(i)-tryptophan isotope labeled amide pairs, and H/D exchange 1H,15N-HSQC experiments conducted in solution, we assigned chemical shifts to all five rhodopsin tryptophan backbone 15N nuclei and partially to their bound protons. 1H,15N chemical shift assignment was achieved for indole side chains of Trp35(1.30) and Trp175(4.65). 15N chemical shifts were found to be similar when comparing those obtained in the native like reconstituted lipid environment and those obtained in detergent micelles for all tryptophans except Trp175(4.65) at the membrane interface. The results suggest that the integrated solution and solid state NMR approach presented provides highly complementary information in the study of structure and dynamics of large membrane proteins like rhodopsin.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.