ArticleJournal of the American Chemical Society2017
Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 37 citations in OpenAlex.
- Article
- SABRE Hyperpolarization with up to 200 bar Parahydrogen in Standard and Quickly Removable Solvents.International journal of molecular sciences · 2023Article
- Elucidating the mechanisms underlying protein conformational switching using NMR spectroscopy.Journal of magnetic resonance open · 2022Article
- Transition-State Compressibility and Activation Volume of Transient Protein Conformational Fluctuations.JACS Au · 2021Article
- Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics.Magnetic resonance (Gottingen, Germany) · 2021Review
- Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- Experimental estimates of compression heating and decompression cooling in ethylene glycol.Magnetic resonance in chemistry : MRC · 2020Article
- Fast electron paramagnetic resonance magic angle spinning simulations using analytical powder averaging techniques.The Journal of chemical physics · 2019Article
- Fast pressure-jump all-atom simulations and experiments reveal site-specific protein dehydration-folding dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Interrupted Pressure-Jump NMR Experiments Reveal Resonances of On-Pathway Protein Folding Intermediate.The journal of physical chemistry. B · 2018Article
- Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology.Methods (San Diego, Calif.) · 2018Article
- MonitoringJournal of the American Chemical Society · 2018Article
- Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Propensity for cis-Proline Formation in Unfolded Proteins.Chembiochem : a European journal of chemical biology · 2018Article
- Additive fabrication for NMR probe builders.Progress in nuclear magnetic resonance spectroscopyReview
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
A method is introduced that permits direct observation of the rates at which backbone amide hydrogens become protected from solvent exchange after rapidly dropping the hydrostatic pressure inside the NMR sample cell from denaturing (2.5 kbar) to native (1 bar) conditions. The method is demonstrated for a pressure-sensitized ubiquitin variant that contains two Val to Ala mutations. Increased protection against hydrogen exchange with solvent is monitored as a function of time during the folding process. Results for 53 backbone amides show narrow clustering with protection occurring with a time constant of ca. 85 ms, but slower protection is observed around a reverse turn near the C-terminus of the protein. Remarkably, the native NMR spectrum returns with this slower time constant of ca. 150 ms, indicating that the almost fully folded protein retains molten globule characteristics with severe NMR line broadening until the final hydrogen bonds are formed. Prior to crossing the transition state barrier, hydrogen exchange protection factors are close to unity, but with slightly elevated values in the β
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