ArticleBiophysical journal2008
Thermal unfolding simulations of bacterial flagellin: insight into its refolding before assembly.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Molecular dynamics simulation of bacterial flagella.Biophysical reviews · 2018Review
- Article
- Insights into the structural stability of Bax from molecular dynamics simulations at high temperatures.Protein science : a publication of the Protein Society · 2011Article
- Theoretical and computational investigation of flagellin translocation and bacterial flagellum growth.Biophysical journal · 2011Article
- Temperature-induced unfolding of epidermal growth factor (EGF): insight from molecular dynamics simulation.Journal of molecular graphics & modelling · 2010Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flagellin is the subunit of the bacterial filament, the micrometer-long propeller of a bacterial flagellum. The protein is believed to undergo unfolding for transport through the channel of the filament and to refold in a chamber at the end of the channel before being assembled into the growing filament. We report a thermal unfolding simulation study of S. typhimurium flagellin in aqueous solution as an attempt to gain atomic-level insight into the refolding process. Each molecule comprises two filament-core domains {D0, D1} and two hypervariable-region domains {D2, D3}. D2 can be separated into subdomains D2a and D2b. We observed a similar unfolding order of the domains as reported in experimental thermal denaturation. D2a and D3 exhibited high thermal stability and contained persistent three-stranded beta-sheets in the denatured state which could serve as folding cores to guide refolding. A recent mutagenesis study on flagellin stability seems to suggest the importance of the folding cores. Using crude size estimates, our data suggests that the chamber might be large enough for either denatured hypervariable-region domains or filament-core domains, but not whole flagellin; this implicates a two-staged refolding process.
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Registered trials
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