ArticleBiophysical journal2006
Prediction of the translocation kinetics of a protein from its mechanical properties.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 37 citations in OpenAlex.
- 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
- Protein unfolding by biological unfoldases: insights from modeling.Biophysical journal · 2014Article
- Mechanical anisotropy of ankyrin repeats.Biophysical journal · 2012Article
- Unfolding and translocation pathway of substrate protein controlled by structure in repetitive allosteric cycles of the ClpY ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations.The Journal of biological chemistry · 2010Article
- An experimentally guided umbrella sampling protocol for biomolecules.The Journal of chemical physics · 2008Article
- Excursion of a single polypeptide into a protein pore: simple physics, but complicated biology.European biophysics journal : EBJ · 2008Article
- An effective strategy for the design of proteins with enhanced mechanical stability.Angewandte Chemie (International ed. in English) · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins are actively unfolded to pass through narrow channels in macromolecular complexes that catalyze protein translocation and degradation. Catalyzed unfolding shares many features that characterize the mechanical unfolding of proteins using the atomic force microscope (AFM). However, simulations of unfolding induced by the AFM and when a protein is translocated through a pore suggest that each process occurs by distinct pathways. The link, if any, between each type of unfolding, therefore, is not known. We show that the mechanical unfolding energy landscape of a protein, obtained using an atomistic molecular model, can be used to predict both the relative mechanical strength of proteins when unfolded using the AFM and when unfolded by translocation into a pore. We thus link the two processes and show that the import rate through a pore not only depends on the location of the initiation tag but also on the mechanical properties of the protein when averaged over all the possible geometries that are relevant for a given translocation initiation site.
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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.