ArticleProceedings of the National Academy of Sciences of the United States of America2006
Identification of the minimal protein-folding nucleus through loop-entropy perturbations.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Design of stable circular permutants of the GroEL chaperone apical domain.Cell communication and signaling : CCS · 2024Article
- Article
- Design and characterization of a protein fold switching network.Nature communications · 2023Article
- Variable and Conserved Regions of Secondary Structure in the β-Trefoil Fold: Structure Versus Function.Frontiers in molecular biosciences · 2022Article
- Exposing the distinctive modular behavior of β-strands and α-helices in folded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Experimental approach to study the effect of mutations on the protein folding pathway.PloS one · 2019Article
- Effects of protein size, thermodynamic stability, and net charge on cotranslational folding on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Evolution of a protein folding nucleus.Protein science : a publication of the Protein Society · 2016Article
- Constructing sequence-dependent protein models using coevolutionary information.Protein science : a publication of the Protein Society · 2016Article
- Fold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus?Journal of the Royal Society, Interface · 2015Article
- The response of Greek key proteins to changes in connectivity depends on the nature of their secondary structure.Journal of molecular biology · 2015Article
- Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?Archives of biochemistry and biophysics · 2014Review
- 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
- Circular permutation of a WW domain: folding still occurs after excising the turn of the folding-nucleating hairpin.Journal of the American Chemical Society · 2014Article
- Take home lessons from studies of related proteins.Current opinion in structural biology · 2013Review
- A "Link-Psi" strategy using crosslinking indicates that the folding transition state of ubiquitin is not very malleable.Protein science : a publication of the Protein Society · 2012Article
- Folding without charges.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Trimming down a protein structure to its bare foldons: spatial organization of the cooperative unit.The Journal of biological chemistry · 2012Article
- Article
- Folding circular permutants of IL-1β: route selection driven by functional frustration.PloS one · 2012Article
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5 authors.
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Abstract
To explore the plasticity and structural constraints of the protein-folding nucleus we have constructed through circular permutation four topological variants of the ribosomal protein S6. In effect, these topological variants represent entropy mutants with maintained spatial contacts. The proteins were characterized at two complementary levels of detail: by phi-value analysis estimating the extent of contact formation in the transition-state ensemble and by Hammond analysis measuring the site-specific growth of the folding nucleus. The results show that, although the loop-entropy alterations markedly influence the appearance and structural location of the folding nucleus, it retains a common motif of one helix docking against two strands. This nucleation motif is built around a shared subset of side chains in the center of the hydrophobic core but extends in different directions of the S6 structure following the permutant-specific differences in local loop entropies. The adjustment of the critical folding nucleus to alterations in loop entropies is reflected by a direct correlation between the phi-value change and the accompanying change in local sequence separation.
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