ArticleProceedings of the National Academy of Sciences of the United States of America2007
Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Ultrafast Nuclear Magnetic Resonance as a Tool to Detect Rapid Chemical Change in Solution.ACS physical chemistry Au · 2024Review
- An Atomistic View on the Mechanism of Diatom Peptide-Guided Biomimetic Silica Formation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Investigating lysozyme amyloid fibril formation and structural variability dependence on its initial folding state under different pH conditions.Protein science : a publication of the Protein Society · 2024Article
- Real-time monitoring of the sialic acid biosynthesis pathway by NMR.Chemical science · 2023Article
- Protein Unfolding in Freeze Frames: Intermediate States are Revealed by Variable-Temperature Ion Mobility-Mass Spectrometry.Analytical chemistry · 2022Article
- CryoFold: determining protein structures and data-guided ensembles from cryo-EM density maps.Matter · 2021Article
- Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens.Scientific reports · 2021Article
- Effects of Ionic Liquids on Metalloproteins.Molecules (Basel, Switzerland) · 2021Review
- Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics.Magnetic resonance (Gottingen, Germany) · 2021Review
- Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways.Molecules (Basel, Switzerland) · 2020Review
- α-Lactalbumin, Amazing Calcium-Binding Protein.Biomolecules · 2020Review
- Structure of an Unfolding Intermediate of an RRM Domain of ETR-3 Reveals Its Native-like Fold.Biophysical journal · 2020Article
- Importance of time-ordered non-uniform sampling of multi-dimensional NMR spectra of AβJournal of biomolecular NMR · 2019Article
- Interrupted Pressure-Jump NMR Experiments Reveal Resonances of On-Pathway Protein Folding Intermediate.The journal of physical chemistry. B · 2018Article
- MonitoringJournal of the American Chemical Society · 2018Article
- Optimized fast mixing device for real-time NMR applications.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2017Article
- Real-Time Analysis of Folding upon Binding of a Disordered Protein by Using Dissolution DNP NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2017Article
- Conformational Flexibility Differentiates Naturally Occurring Bet v 1 Isoforms.International journal of molecular sciences · 2017Article
- RNA binding and chaperone activity of the E. coli cold-shock protein CspA.Nucleic acids research · 2017Article
- Unraveling self-assembly pathways of the 468-kDa proteolytic machine TET2.Science advances · 2017Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Atom-resolved real-time studies of kinetic processes in proteins have been hampered in the past by the lack of experimental techniques that yield sufficient temporal and atomic resolution. Here we present band-selective optimized flip-angle short transient (SOFAST) real-time 2D NMR spectroscopy, a method that allows simultaneous observation of reaction kinetics for a large number of nuclear sites along the polypeptide chain of a protein with an unprecedented time resolution of a few seconds. SOFAST real-time 2D NMR spectroscopy combines fast NMR data acquisition techniques with rapid sample mixing inside the NMR magnet to initiate the kinetic event. We demonstrate the use of SOFAST real-time 2D NMR to monitor the conformational transition of alpha-lactalbumin from a molten globular to the native state for a large number of amide sites along the polypeptide chain. The kinetic behavior observed for the disappearance of the molten globule and the appearance of the native state is monoexponential and uniform along the polypeptide chain. This observation confirms previous findings that a single transition state ensemble controls folding of alpha-lactalbumin from the molten globule to the native state. In a second application, the spontaneous unfolding of native ubiquitin under nondenaturing conditions is characterized by amide hydrogen exchange rate constants measured at high pH by using SOFAST real-time 2D NMR. Our data reveal that ubiquitin unfolds in a gradual manner with distinct unfolding regimes.
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