ArticleJournal of molecular biology2009
Different members of a simple three-helix bundle protein family have very different folding rate constants and fold by different mechanisms.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- The transition state for coupled folding and binding of a disordered DNA binding domain resembles the unbound state.Nucleic acids research · 2024Article
- Protein folding problem: enigma, paradox, solution.Biophysical reviews · 2022Review
- Cotranslational folding cooperativity of contiguous domains of α-spectrin.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- PFDB: A standardized protein folding database with temperature correction.Scientific reports · 2019Article
- Sequence-, structure-, and dynamics-based comparisons of structurally homologous CheY-like proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Modulation of Folding Internal Friction by Local and Global Barrier Heights.The journal of physical chemistry letters · 2016Article
- Protein unfolding rates correlate as strongly as folding rates with native structure.Protein science : a publication of the Protein Society · 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
- Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- General mechanism of two-state protein folding kinetics.Journal of the American Chemical Society · 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
- Mechanism of assembly of the non-covalent spectrin tetramerization domain from intrinsically disordered partners.Journal of molecular biology · 2014Article
- How well does a funneled energy landscape capture the folding mechanism of spectrin domains?The journal of physical chemistry. B · 2013Article
- Understanding pathogenic single-nucleotide polymorphisms in multidomain proteins--studies of isolated domains are not enough.The FEBS journal · 2013Article
- Take home lessons from studies of related proteins.Current opinion in structural biology · 2013Review
- Polymer uncrossing and knotting in protein folding, and their role in minimal folding pathways.PloS one · 2013Article
- Slow, reversible, coupled folding and binding of the spectrin tetramerization domain.Biophysical journal · 2012Article
- Separating the effects of internal friction and transition state energy to explain the slow, frustrated folding of spectrin domains.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Protein folding: adding a nucleus to guide helix docking reduces landscape roughness.Journal of molecular biology · 2012Article
- The denatured state dictates the topology of two proteins with almost identical sequence but different native structure and function.The Journal of biological chemistry · 2011Article
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Authors and funding
5 authors.
Funding
Abstract
The 15th, 16th, and 17th repeats of chicken brain alpha-spectrin (R15, R16, and R17, respectively) are very similar in terms of structure and stability. However, R15 folds and unfolds 3 orders of magnitude faster than R16 and R17. This is unexpected. The rate-limiting transition state for R15 folding is investigated using protein engineering methods (Phi-value analysis) and compared with previously completed analyses of R16 and R17. Characterisation of many mutants suggests that all three proteins have similar complexity in the folding landscape. The early rate-limiting transition states of the three domains are similar in terms of overall structure, but there are significant differences in the patterns of Phi-values. R15 apparently folds via a nucleation-condensation mechanism, which involves concomitant folding and packing of the A- and C-helices, establishing the correct topology. R16 and R17 fold via a more framework-like mechanism, which may impede the search to find the correct packing of the helices, providing a possible explanation for the fast folding of R15.
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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.