ArticleProtein science : a publication of the Protein Society2006
Cooperativity and the origins of rapid, single-exponential kinetics in protein folding.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Folding and knotting of biotic and prebiotic amino acid sequences through reverse evolution.Biophysical journal · 2025Article
- Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different.Journal of molecular biology · 2020Review
- Article
- Probing the origins of two-state folding.The Journal of chemical physics · 2013Article
- Helix/coil nucleation: a local response to global demands.Biophysical journal · 2009Article
- Effective knowledge-based potentials.Protein science : a publication of the Protein Society · 2009Article
- What have we learned from the studies of two-state folders, and what are the unanswered questions about two-state protein folding?Physical biology · 2009Article
- Direct measurement of tertiary contact cooperativity in RNA folding.Journal of the American Chemical Society · 2008Article
- Predicting coupling limits from an experimentally determined energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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2 authors.
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Abstract
The folding of naturally occurring, single-domain proteins is usually well described as a simple, single-exponential process lacking significant trapped states. Here we further explore the hypothesis that the smooth energy landscape this implies, and the rapid kinetics it engenders, arises due to the extraordinary thermodynamic cooperativity of protein folding. Studying Miyazawa-Jernigan lattice polymers, we find that, even under conditions where the folding energy landscape is relatively optimized (designed sequences folding at their temperature of maximum folding rate), the folding of protein-like heteropolymers is accelerated when their thermodynamic cooperativity is enhanced by enhancing the nonadditivity of their energy potentials. At lower temperatures, where kinetic traps presumably play a more significant role in defining folding rates, we observe still greater cooperativity-induced acceleration. Consistent with these observations, we find that the folding kinetics of our computational models more closely approximates single-exponential behavior as their cooperativity approaches optimal levels. These observations suggest that the rapid folding of naturally occurring proteins is, in part, a consequence of their remarkably cooperative folding.
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