ArticleProtein science : a publication of the Protein Society2012
Is there an en route folding intermediate for Cold shock proteins?
Article in Protein science : a publication of the Protein Society, 2012. 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.
- A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution.Nature communications · 2016Article
- Statistical dictionaries for hypothetical in silico model of the early-stage intermediate in protein folding.Journal of computer-aided molecular design · 2015Article
- A simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior.PLoS computational biology · 2014Article
- Probing the protein-folding mechanism using denaturant and temperature effects on rate constants.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Assessing the effect of loop mutations in the folding space of β2-microglobulin with molecular dynamics simulations.International journal of molecular sciences · 2013Article
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2 authors.
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Abstract
Cold shock proteins (Csps) play an important role in cold shock response of a diverse number of organisms ranging from bacteria to humans. Numerous studies of the Csp from various species showed that a two-state folding mechanism is conserved and the transition state (TS) appears to be very compact. However, the atomic details of the folding mechanism of Csp remain unclear. This study presents the folding mechanism of Csp in atomic detail using an all-atom Go model-based simulations. Our simulations predict that there may exist an en route intermediate, in which β strands 1-2-3 are well ordered and the contacts between β1 and β4 are almost developed. Such an intermediate might be too unstable to be detected in the previous fluorescence energy transfer experiments. The transition state ensemble has been determined from the P(fold) analysis and the TS appears even more compact than the intermediate state.
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