ArticleProteins2008
How general is the nucleation-condensation mechanism?
Article in Proteins, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 36 citations in OpenAlex.
- FoldPAthreader: predicting protein folding pathway using a novel folding force field model derived from known protein universe.Genome biology · 2024Article
- Slowest-first protein translation scheme: Structural asymmetry and co-translational folding.Biophysical journal · 2021Article
- A look back at the molten globule state of proteins: thermodynamic aspects.Biophysical reviews · 2019Review
- Molecular recognition and packing frustration in a helical protein.PLoS computational biology · 2017Article
- Protein Folding Structures: Formation of Folding Structures Based on Probability Theory.ACS omega · 2016Article
- Folding analysis of the most complex Stevedore's protein knot.Scientific reports · 2016Article
- Evolution of a protein folding nucleus.Protein science : a publication of the Protein Society · 2016Article
- Characterization of protein folding by a Φ-value calculation with a statistical-mechanical model.Biophysics and physicobiology · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We investigate the structures of the major folding transition states of nine proteins by correlation of published Phi-values with inter-residue contact maps. Combined with previous studies on six proteins, the analysis suggests that at least 10 of the 15 small globular proteins fold via a nucleation-condensation mechanism with a concurrent build-up of secondary and tertiary structure contacts, but a structural consolidation that is clearly nonuniformly distributed over the molecule and most intense in a single structural region suggesting the occurrence of a single folding nucleus. However, on average helix- and sheet-forming residues show somewhat larger Phi-values in the major transition state, suggesting that secondary structure formation is one important driving force in the nucleation-condensation in many proteins and that secondary-structure forming residues tend to be more prominent in folding nuclei. We synthesize the combined information on these 10 of 15 proteins into a unified nucleation-condensation mechanism which also accounts for effects described by the framework, hydrophobic collapse, zipper, and funnel models.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.