ArticleJournal of the American Chemical Society2014
Circular permutation of a WW domain: folding still occurs after excising the turn of the folding-nucleating hairpin.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnChembiochem : a European journal of chemical biology · 2023Article
- Identification of novel functional mini-receptors by combinatorial screening of split-WW domains.Chemical science · 2022Article
- Investigating the Effect of Chain Connectivity on the Folding of a Beta-Sheet Protein On and Off the Ribosome.Journal of molecular biology · 2018Article
- A pH Switch for β-Sheet Protein Folding.Angewandte Chemie (International ed. in English) · 2017Article
- Optimization of a β-sheet-cap for long loop closure.Biopolymers · 2017Article
- Aryl-aryl interactions in designed peptide folds: Spectroscopic characteristics and optimal placement for structure stabilization.Biopolymers · 2016Article
- An improved capping unit for stabilizing the ends of associated β-strands.FEBS letters · 2014Article
- Folding dynamics and pathways of the trp-cage miniproteins.Biochemistry · 2014Article
- Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
A hyperstable Pin1 WW domain has been circularly permuted via excision of the fold-nucleating turn; it still folds to form the native three-strand sheet and hydrophobic core features. Multiprobe folding dynamics studies of the normal and circularly permuted sequences, as well as their constituent hairpin fragments and comparable-length β-strand-loop-β-strand models, indicate 2-state folding for all topologies. N-terminal hairpin formation is the fold nucleating event for the wild-type sequence; the slower folding circular permutant has a more distributed folding transition state.
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Registered trials
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