ArticleProceedings of the National Academy of Sciences of the United States of America2011
Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- AI-Resolved Protein Energy Landscapes, Electrodynamics, and Fluidic Microcircuits as a Unified Framework for Predicting Neurodegeneration.International journal of molecular sciences · 2026Review
- Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding.Molecules (Basel, Switzerland) · 2023Review
- Transient On- and Off-Pathway Protein Folding Intermediate States Characterized with NMR Relaxation Dispersion.The journal of physical chemistry. B · 2022Article
- Single-molecule biophysics experimentsiScience · 2022Article
- Native state fluctuations in a peroxiredoxin active site match motions needed for catalysis.Structure (London, England : 1993) · 2022Article
- Minimizing Pervasive Artifacts in 4D Covariance Maps for Protein Side Chain NMR Assignments.The journal of physical chemistry. A · 2021Article
- Real-time tracking of protein unfolding with time-resolved x-ray solution scattering.Structural dynamics (Melville, N.Y.) · 2020Article
- Compact expressions for RJournal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- Determining Binding Kinetics of Intrinsically Disordered Proteins by NMR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Chemical Exchange.Methods in enzymology · 2019Article
- Article
- Nanopore Sensing of Protein Folding.ACS nano · 2017Article
- Practical considerations for investigation of protein conformational dynamics byJournal of biomolecular NMR · 2017Article
- How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway.Accounts of chemical research · 2017Article
- Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
- Visualizing the formation of an RNA folding intermediate through a fast highly modular secondary structure switch.Nature communications · 2016Article
- Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.Physical chemistry chemical physics : PCCP · 2016Article
- Extracting protein dynamics information from overlapped NMR signals using relaxation dispersion difference NMR spectroscopy.Journal of biomolecular NMR · 2015Article
- Evidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Probing the non-native H helix translocation in apomyoglobin folding intermediates.Biochemistry · 2014Article
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2 authors.
Funding
Abstract
Detailed understanding of protein function and malfunction hinges on the ability to characterize transiently populated states and the transitions between them. Here, we use (15)N, , and (13)CO NMR R(2) relaxation dispersion to investigate spontaneous unfolding and refolding events of native apomyoglobin. Above pH 5.0, dispersion is dominated by processes involving fluctuations of the F-helix region, which is invisible in NMR spectra. Measurements of R(2) dispersion for residues contacted by the F-helix region in the native (N) structure reveal a transient state formed by local unfolding of helix F and undocking from the protein core. A similar state was detected at pH 4.75-4.95 and determined to be an on-pathway intermediate (I1) in a linear three-state unfolding scheme (N&lrarr2;I1&lrarr2;MG) leading to a transiently populated molten globule (MG) state. The slowest steps in unfolding and refolding are N → I1 (36 s(-1)) and MG → I1 (26 s(-1)), respectively. Differences in chemical shift between N and I1 are very small, except in regions adjacent to helix F, showing that their core structures are similar. Chemical shift changes between the N and MG states, obtained from R(2) dispersion, reveal that the transient MG state is structurally similar to the equilibrium MG observed previously at high temperature and low pH. Analysis of MG state chemical shifts shows the location of residual helical structure in the transient intermediate and identifies regions that unfold or rearrange into nonnative structure during the N → MG transition. The experiments also identify regions of energetic frustration that "crack" during unfolding and impede the refolding process.
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