ArticleProtein science : a publication of the Protein Society2003
Contact order revisited: influence of protein size on the folding rate.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers.
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136 citing papers in PubMed, 374 citations in OpenAlex.
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- On the free energy of protein folding in optical tweezers experiments.Biophysical reviews · 2025Review
- Importance of Inter-residue Contacts for Understanding Protein Folding and Unfolding Rates, Remote Homology, and Drug Design.Molecular biotechnology · 2025Review
- Co-translational protein aggregation and ribosome stalling as a broad-spectrum antibacterial mechanism.Nature communications · 2025Article
- Folds from fold: Exploring topological isoforms of a single-domain protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- On the role of native contact cooperativity in protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The dynamic-process characterization and prediction of synthetic gene circuits by dynamic delay model.iScience · 2024Article
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- Folding kinetics of an entangled protein.PLoS computational biology · 2023Article
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- FungiProteomeDB: a database for the molecular weight and isoelectric points of the fungal proteomes.Database : the journal of biological databases and curation · 2023Article
- Engineering the kinetic stability of a β-trefoil protein by tuning its topological complexity.Frontiers in molecular biosciences · 2023Article
- Protein folding problem: enigma, paradox, solution.Biophysical reviews · 2022Review
76 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Guided by the recent success of empirical model predicting the folding rates of small two-state folding proteins from the relative contact order (CO) of their native structures, by a theoretical model of protein folding that predicts that logarithm of the folding rate decreases with the protein chain length L as L(2/3), and by the finding that the folding rates of multistate folding proteins strongly correlate with their sizes and have very bad correlation with CO, we reexamined the dependence of folding rate on CO and L in attempt to find a structural parameter that determines folding rates for the totality of proteins. We show that the Abs_CO = CO x L, is able to predict rather accurately folding rates for both two-state and multistate folding proteins, as well as short peptides, and that this Abs_CO scales with the protein chain length as L(0.70 +/- 0.07) for the totality of studied single-domain proteins and peptides.
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