ArticleThe Journal of chemical physics2013
Probing the origins of two-state folding.
Article in The Journal of chemical physics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Unsupervised Learning Methods for Molecular Simulation Data.Chemical reviews · 2021Article
- Influence of Glu/Arg, Asp/Arg, and Glu/Lys Salt Bridges on α-Helical Stability and Folding Kinetics.Biophysical journal · 2016Article
- First Passage Times, Lifetimes, and Relaxation Times of Unfolded Proteins.Physical review letters · 2015Article
- A compact native 24-residue supersecondary structure derived from the villin headpiece subdomain.Biophysical journal · 2015Article
- Intermediates in the folding equilibrium of repeat proteins from the TPR family.European biophysics journal : EBJ · 2014Article
- Complex pathways in folding of protein G explored by simulation and experiment.Biophysical journal · 2014Article
- Inferring Microscopic Kinetic Rates from Stationary State Distributions.Journal of chemical theory and computation · 2014Article
- Solvent-Exposed Salt Bridges Influence the Kinetics of α-Helix Folding and Unfolding.The journal of physical chemistry letters · 2014Article
- How long does it take to equilibrate the unfolded state of a protein?Protein science : a publication of the Protein Society · 2013Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Many protein systems fold in a two-state manner. Random models, however, rarely display two-state kinetics and thus such behavior should not be accepted as a default. While theories for the prevalence of two-state kinetics have been presented, none sufficiently explain the breadth of experimental observations. A model, making minimal assumptions, is introduced that suggests two-state behavior is likely for any system with an overwhelmingly populated native state. We show two-state folding is a natural consequence of such two-state thermodynamics, and is strengthened by increasing the population of the native state. Further, the model exhibits hub-like behavior, with slow interconversions between unfolded states. Despite this, the unfolded state equilibrates quickly relative to the folding time. This apparent paradox is readily understood through this model. Finally, our results compare favorable with measurements of folding rates as a function of chain length and Keq, providing new insight into these relations.
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Registered trials
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