ArticleJournal of molecular biology2008
The folding pathway of a single domain in a multidomain protein is not affected by its neighbouring domain.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Determinants of Protein Folding Pathways: Lessons from Metamorphic Proteins.International journal of molecular sciences · 2026Review
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- Spectroscopic analysis of the bacterially expressed head domain of rotavirus VP6.Bioscience reports · 2024Article
- Folding pathway of a discontinuous two-domain protein.Nature communications · 2024Article
- The New Functional Hybrid Chaperone Protein ADGroEL-SacSm.Molecules (Basel, Switzerland) · 2023Article
- Domain tethering impacts dimerization and DNA-mediated allostery in the human transcription factor FoxP1.The Journal of chemical physics · 2023Article
- Cotranslational folding cooperativity of contiguous domains of α-spectrin.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Energetic dependencies dictate folding mechanism in a complex protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Studying the folding of multidomain proteins.HFSP journal · 2008Article
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Authors and funding
2 authors.
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Abstract
Domains are the structural, functional, and evolutionary components of proteins. Most folding studies to date have concentrated on the folding of single domains, but more than 70% of human proteins contain more than one domain, and interdomain interactions can affect both the stability and the folding kinetics. Whether the folding pathway is altered by interdomain interactions is not yet known. Here we investigated the effect of a folded neighbouring domain on the folding pathway of spectrin R16 (the 16th alpha-helical repeat from chicken brain alpha-spectrin) by using the two-domain construct R1516. The R16 folds faster and unfolds more slowly in the presence of its folded neighbour R15 (the 15th alpha-helical repeat from chicken brain alpha-spectrin). An extensive Phi-value analysis of the R16 domain in R1516 was completed to compare the transition state of the R16 domain alone with that of the R16 domain in a multidomain construct. The results indicate that the folding pathways are the same. This result validates the current approach of breaking up larger proteins into domains for the study of protein folding pathways.
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