ArticleProceedings of the National Academy of Sciences of the United States of America2007
A PDZ domain recapitulates a unifying mechanism for protein folding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Determinants of Protein Folding Pathways: Lessons from Metamorphic Proteins.International journal of molecular sciences · 2026Review
- Inferring protein-folding mechanisms from natural sequence diversity.Biophysical journal · 2025Article
- A Glimpse into the Structural Properties of the Intermediate and Transition State in the Folding of Bromodomain 2 Domain 2 by Φ Value Analysis.International journal of molecular sciences · 2021Article
- The Conformational Plasticity Vista of PDZ Domains.Life (Basel, Switzerland) · 2020Review
- A structurally heterogeneous transition state underlies coupled binding and folding of disordered proteins.The Journal of biological chemistry · 2019Article
- How Many Protein Sequences Fold to a Given Structure? A Coevolutionary Analysis.Biophysical journal · 2017Article
- Some (dis)assembly required: partial unfolding in the Par-6 allosteric switch.Biophysical reviews · 2015Article
- Understanding the effect of alternative splicing in the folding and function of the second PDZ from protein tyrosine phosphatase-BL.Scientific reports · 2015Article
- Contribution to the prediction of the fold code: application to immunoglobulin and flavodoxin cases.PloS one · 2015Article
- Understanding the frustration arising from the competition between function, misfolding, and aggregation in a globular protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Periaxin and AHNAK nucleoprotein 2 form intertwined homodimers through domain swapping.The Journal of biological chemistry · 2014Article
- The folding of a family of three-helix bundle proteins: spectrin R15 has a robust folding nucleus, unlike its homologous neighbours.Journal of molecular biology · 2014Article
- The role of backbone hydrogen bonds in the transition state for protein folding of a PDZ domain.PloS one · 2014Article
- Allosteric activation of the Par-6 PDZ via a partial unfolding transition.Journal of the American Chemical Society · 2013Article
- Equilibrium unfolding of the PDZ domain of β2-syntrophin.Biophysical journal · 2012Article
- Article
- Sequence-specific long range networks in PSD-95/discs large/ZO-1 (PDZ) domains tune their binding selectivity.The Journal of biological chemistry · 2011Article
- Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain.Nature structural & molecular biology · 2010Article
- Crystallographic and nuclear magnetic resonance evaluation of the impact of peptide binding to the second PDZ domain of protein tyrosine phosphatase 1E.Biochemistry · 2010Article
- What lessons can be learned from studying the folding of homologous proteins?Methods (San Diego, Calif.) · 2010Review
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8 authors.
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Abstract
A unifying view has been recently proposed according to which the classical diffusion-collision and nucleation-condensation models may represent two extreme manifestations of an underlying common mechanism for the folding of small globular proteins. We report here the characterization of the folding process of the PDZ domain, a protein that recapitulates the three canonical steps involved in this unifying mechanism, namely: (i) the early formation of a weak nucleus that determines the native-like topology of a large portion of the structure, (ii) a global collapse of the entire polypeptide chain, and (iii) the consolidation of the remaining partially structured regions to achieve the native state conformation. These steps, which are clearly detectable in the PDZ domain investigated here, may be difficult to distinguish experimentally in other proteins, which would thus appear to follow one of the two limiting mechanisms. The analysis of the (un)folding kinetics for other three-state proteins (when available) appears consistent with the predictions ensuing from this unifying mechanism, thus providing a powerful validation of its general nature.
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