ArticleJournal of the American Chemical Society2011
Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study.
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 18 papers.
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Who cites it
18 citing papers in PubMed.
- Making invisible excited-state structures of pro-interleukin-18 visible by combining NMR and machine learning.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mapping the FF domain folding pathway via structures of transiently populated folding intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Probing excited stateMethods (San Diego, Calif.) · 2023Article
- Transient On- and Off-Pathway Protein Folding Intermediate States Characterized with NMR Relaxation Dispersion.The journal of physical chemistry. B · 2022Article
- Structural-Energetic Basis for Coupling between Equilibrium Fluctuations and Phosphorylation in a Protein Native Ensemble.ACS central science · 2022Article
- The A39G FF domain folds on a volcano-shaped free energy surface via separate pathways.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Measuring radiofrequency fields in NMR spectroscopy using offset-dependent nutation profiles.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2021Article
- Slow Folding of a Helical Protein: Large Barriers, Strong Internal Friction, or a Shallow, Bumpy Landscape?The journal of physical chemistry. B · 2020Article
- Atomic structures of excited state A-T Hoogsteen base pairs in duplex DNA by combining NMR relaxation dispersion, mutagenesis, and chemical shift calculations.Journal of biomolecular NMR · 2018Article
- Atomistic structural ensemble refinement reveals non-native structure stabilizes a sub-millisecond folding intermediate of CheY.Scientific reports · 2017Article
- When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches.The Biochemical journal · 2016Review
- Evaluating the influence of initial magnetization conditions on extracted exchange parameters in NMR relaxation experiments: applications to CPMG and CEST.Journal of biomolecular NMR · 2016Article
- NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Defining a length scale for millisecond-timescale protein conformational exchange.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain.PloS one · 2013Article
- Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Transiently populated intermediate functions as a branching point of the FF domain folding pathway.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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7 authors.
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Abstract
Several all-helical single-domain proteins have been shown to fold rapidly (microsecond time scale) to a compact intermediate state and subsequently rearrange more slowly to the native conformation. An understanding of this process has been hindered by difficulties in experimental studies of intermediates in cases where they are both low-populated and only transiently formed. One such example is provided by the on-pathway folding intermediate of the small four-helix bundle FF domain from HYPA/FBP11 that is populated at several percent with a millisecond lifetime at room temperature. Here we have studied the L24A mutant that has been shown previously to form nonnative interactions in the folding transition state. A suite of Carr-Purcell-Meiboom-Gill relaxation dispersion NMR experiments have been used to measure backbone chemical shifts and amide bond vector orientations of the invisible folding intermediate that form the input restraints in calculations of atomic resolution models of its structure. Despite the fact that the intermediate structure has many features that are similar to that of the native state, a set of nonnative contacts is observed that is even more extensive than noted previously for the wild-type (WT) folding intermediate. Such nonnative interactions, which must be broken prior to adoption of the native conformation, explain why the transition from the intermediate state to the native conformer (millisecond time scale) is significantly slower than from the unfolded ensemble to the intermediate and why the L24A mutant folds more slowly than the WT.
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