ArticleProceedings of the National Academy of Sciences of the United States of America2001
An amino acid code for protein folding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Structural Biology in the AlphaFold Era: How Far Is Artificial Intelligence from Deciphering the Protein Folding Code?Biomolecules · 2025Review
- Protein aggregates and biomolecular condensates: implications for human health and disease.Frontiers in molecular biosciences · 2025Review
- Global Patterns of Subgenome Evolution in Organelle-Targeted Genes of Six Allotetraploid Angiosperms.Molecular biology and evolution · 2022Article
- Cytochrome c: Using Biological Insight toward Engineering an Optimized Anticancer Biodrug.Inorganics · 2021Article
- Protein folding - seeing is deceiving.Protein science : a publication of the Protein Society · 2021Article
- Looking Beyond the Core: The Role of Flanking Regions in the Aggregation of Amyloidogenic Peptides and Proteins.Frontiers in neuroscience · 2020Review
- Paramagnetic relaxation enhancement-assisted structural characterization of a partially disordered conformation of ubiquitin.Protein science : a publication of the Protein Society · 2019Article
- Article
- Protein Folding Structures: Formation of Folding Structures Based on Probability Theory.ACS omega · 2016Article
- The role of the backbone torsion in protein folding.Biology direct · 2016Article
- How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016Review
- UniCon3D: de novo protein structure prediction using united-residue conformational search via stepwise, probabilistic sampling.Bioinformatics (Oxford, England) · 2016Article
- Network representation of conformational transitions between hidden intermediates of Rd-apocytochrome b562.The Journal of chemical physics · 2015Article
- General mechanism of two-state protein folding kinetics.Journal of the American Chemical Society · 2014Article
- Measurement of histidine pKa values and tautomer populations in invisible protein states.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- NMR investigations on residue level unfolding thermodynamics in DLC8 dimer by temperature dependent native state hydrogen exchange.Journal of biomolecular NMR · 2009Article
- Lack of cytochrome c in mouse fibroblasts disrupts assembly/stability of respiratory complexes I and IV.The Journal of biological chemistry · 2009Article
- Protein folding: independent unrelated pathways or predetermined pathway with optional errors.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
Corrections and comments
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4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Direct structural information obtained for many proteins supports the following conclusions. The amino acid sequences of proteins can stabilize not only the final native state but also a small set of discrete partially folded native-like intermediates. Intermediates are formed in steps that use as units the cooperative secondary structural elements of the native protein. Earlier intermediates guide the addition of subsequent units in a process of sequential stabilization mediated by native-like tertiary interactions. The resulting stepwise self-assembly process automatically constructs a folding pathway, whether linear or branched. These conclusions are drawn mainly from hydrogen exchange-based methods, which can depict the structure of infinitesimally populated folding intermediates at equilibrium and kinetic intermediates with subsecond lifetimes. Other kinetic studies show that the polypeptide chain enters the folding pathway after an initial free-energy-uphill conformational search. The search culminates by finding a native-like topology that can support forward (native-like) folding in a free-energy-downhill manner. This condition automatically defines an initial transition state, the search for which sets the maximum possible (two-state) folding rate. It also extends the sequential stabilization strategy, which depends on a native-like context, to the first step in the folding process. Thus the native structure naturally generates its own folding pathway. The same amino acid code that translates into the final equilibrium native structure-by virtue of propensities, patterning, secondary structural cueing, and tertiary context-also produces its kinetic accessibility.
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