ArticleProceedings of the National Academy of Sciences of the United States of America2011
Speed limit of protein folding evidenced in secondary structure dynamics.
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 14 papers.
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Who cites it
14 citing papers in PubMed.
- Article
- Transactivation domain of Adenovirus Early Region 1A (E1A): Investigating folding dynamics and aggregation.Current research in structural biology · 2022Article
- Dissecting Multiple Pathways in the Relaxation Dynamics of Helix <==> Coil Transitions with Optimum Dimensionality Reduction.Biomolecules · 2021Review
- Protons Are Fast and Smart; Proteins Are Slow and Dumb: On the Relationship of Electrospray Ionization Charge States and Conformations.Journal of the American Society for Mass Spectrometry · 2021Article
- Length Dependent Folding Kinetics of Alanine-Based Helical Peptides from Optimal Dimensionality Reduction.Life (Basel, Switzerland) · 2021Article
- Directly monitor protein rearrangement on a nanosecond-to-millisecond time-scale.Scientific reports · 2017Article
- Meandering Down the Energy Landscape of Protein Folding: Are We There Yet?Biophysical journal · 2016Review
- Observation of α-Helical Hydrogen-Bond Cooperativity in an Intact Protein.Journal of the American Chemical Society · 2016Article
- Dominance of misfolded intermediates in the dynamics of α-helix folding.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Effects of side chains in helix nucleation differ from helix propagation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A membrane-proximal, C-terminal α-helix is required for plasma membrane localization and function of the G Protein-coupled receptor (GPCR) TGR5.The Journal of biological chemistry · 2014Article
- Automated Optimization of Potential Parameters.Journal of chemical theory and computation · 2013Article
- Testing the diffusing boundary model for the helix-coil transition in peptides.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Residue-specific α-helix propensities from molecular simulation.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As the simplest and most prevalent motif of protein folding, α-helix initiation is the starting point of macromolecular complexity. In this work, helix initiation was directly measured via ultrafast temperature-jump spectroscopy on the smallest possible helix nucleus for which only the first turn is formed. The rate's dependence on sequence, length, and temperature reveals the fastest possible events in protein folding dynamics, and it was possible to separate the rate-limiting torsional (conformational) diffusion from the fast annealing of the helix. An analytic coarse-grained model for this process, which predicts the initiation rate as a function of temperature, confirms this picture. Moreover, the stipulations of the model were verified by ensemble-converging all-atom molecular dynamics simulations, which reproduced both the picosecond annealing and the nanosecond diffusion processes observed experimentally.
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