ArticleBiophysical journal2014
Protein unfolding by biological unfoldases: insights from modeling.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Factors underlying asymmetric pore dynamics of disaggregase and microtubule-severing AAA+ machines.Biophysical journal · 2021Article
- RNA Pore Translocation with Static and Periodic Forces: Effect of Secondary and Tertiary Elements on Process Activation and Duration.The journal of physical chemistry. B · 2021Article
- The SecA motor generates mechanical force during protein translocation.Nature communications · 2020Article
- Free-energy landscapes of membrane co-translocational protein unfolding.Communications biology · 2020Article
- Periodic forces trigger knot untying during translocation of knotted proteins.Scientific reports · 2016Article
- Coarse-Grained Simulations of Topology-Dependent Mechanisms of Protein Unfolding and Translocation Mediated by ClpY ATPase Nanomachines.PLoS computational biology · 2016Article
- Nonspecific yet decisive: Ubiquitination can affect the native-state dynamics of the modified protein.Protein science : a publication of the Protein Society · 2015Article
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Authors and funding
4 authors.
Funding
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Abstract
The molecular determinants of the high efficiency of biological machines like unfoldases (e.g., the proteasome) are not well understood. We propose a model to study protein translocation into the chamber of biological unfoldases represented as a funnel. It is argued that translocation is a much faster way of unfolding a protein than end-to-end stretching, especially in a low-force regime, because it allows for a conformational freedom while concentrating local tension on consecutive regions of a protein chain and preventing refolding. This results in a serial unfolding of the protein structures dominated by unzipping. Thus, pulling against the unfoldase pore is an efficient catalyst of the unfolding reaction. We also show that the presence of the funnel makes the tension along the backbone of the substrate protein nonuniform even when the protein gets unfolded. Hence, the stalling force measured by single-molecule force spectroscopy techniques may be smaller than the traction force of the unfoldase motor.
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