ArticleJournal of the American Chemical Society2011
Translational diffusion of macromolecular assemblies measured using transverse-relaxation-optimized pulsed field gradient NMR.
Article in Journal of the American Chemical Society, 2011. 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.
- Mispacking of the F87 sidechain drives aggregation-promoting conformational fluctuations in the subunit interfaces of the transthyretin tetramer.Protein science : a publication of the Protein Society · 2024Article
- Autoinhibition in the Signal Transducer CIN85 Modulates B Cell Activation.Journal of the American Chemical Society · 2024Article
- Effect of Ligands and Transducers on the Neurotensin Receptor 1 Conformational Ensemble.Journal of the American Chemical Society · 2022Article
- Snapshots and ensembles of BTK and cIAP1 protein degrader ternary complexes.Nature chemical biology · 2021Article
- High-Resolution Diffusion Measurements of Proteins by NMR under Near-Physiological Conditions.Analytical chemistry · 2020Article
- Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- Measuring translational diffusion ofEuropean biophysics journal : EBJ · 2018Article
- Fluorotryptophan Incorporation Modulates the Structure and Stability of Transthyretin in a Site-Specific Manner.Biochemistry · 2017Article
- An enhanced sensitivity methylJournal of biomolecular NMR · 2017Article
- Ligand-Receptor Interaction Modulates the Energy Landscape of Enzyme-Instructed Self-Assembly of Small Molecules.Journal of the American Chemical Society · 2016Article
- Micro-scale NMR Experiments for Monitoring the Optimization of Membrane Protein Solutions for Structural Biology.Bio-protocol · 2015Article
- Measuring translational diffusion coefficients of peptides and proteins by PFG-NMR using band-selective RF pulses.European biophysics journal : EBJ · 2014Article
- Solution-NMR characterization of outer-membrane protein A from E. coli in lipid bilayer nanodiscs and detergent micelles.Chembiochem : a European journal of chemical biology · 2014Article
- β2-Adrenergic receptor solutions for structural biology analyzed with microscale NMR diffusion measurements.Angewandte Chemie (International ed. in English) · 2013Article
- Radiation damping in modern NMR experiments: progress and challenges.Progress in nuclear magnetic resonance spectroscopy · 2013Article
- Micro-coil NMR to monitor optimization of the reconstitution conditions for the integral membrane protein OmpW in detergent micelles.Journal of biomolecular NMR · 2012Article
- Translational diffusion measurements by microcoil NMR in aqueous solutions of the Fos-10 detergent-solubilized membrane protein OmpX.The journal of physical chemistry. B · 2012Article
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3 authors.
Funding
Abstract
In structural biology, pulsed field gradient (PFG) NMR spectroscopy for the characterization of size and hydrodynamic parameters of macromolecular solutes has the advantage over other techniques that the measurements can be recorded with identical solution conditions as used for NMR structure determination or for crystallization trials. This paper describes two transverse-relaxation-optimized (TRO) (15)N-filtered PFG stimulated-echo (STE) experiments for studies of macromolecular translational diffusion in solution, (1)H-TRO-STE and (15)N-TRO-STE, which include CRINEPT and TROSY elements. Measurements with mixed micelles of the Escherichia coli outer membrane protein X (OmpX) and the detergent Fos-10 were used for a systematic comparison of (1)H-TRO-STE and (15)N-TRO-STE with conventional (15)N-filtered STE experimental schemes. The results provide an extended platform for evaluating the NMR experiments available for diffusion measurements in structural biology projects involving molecular particles with different size ranges. An initial application of the (15)N-TRO-STE experiment with very long diffusion delays showed that the tedradecamer structure of the 800 kDa Thermus thermophilus chaperonin GroEL is preserved in aqueous solution over the temperature range 25-60 °C.
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