ArticleJournal of molecular biology2007
Experiments suggest that simulations may overestimate electrostatic contributions to the mechanical stability of a fibronectin type III domain.
Article in Journal of molecular biology, 2007. 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.
- Contribution of hydrophobic interactions to protein mechanical stability.Computational and structural biotechnology journal · 2022Article
- Single molecule force spectroscopy reveals that electrostatic interactions affect the mechanical stability of proteins.Biophysical journal · 2011Article
- Water's role in the force-induced unfolding of ubiquitin.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Changing the mechanical unfolding pathway of FnIII10 by tuning the pulling strength.Biophysical journal · 2009Article
- Fibronectin unfolding revisited: modeling cell traction-mediated unfolding of the tenth type-III repeat.PloS one · 2008Article
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Authors and funding
2 authors.
Funding
Abstract
Steered molecular dynamics simulations have previously been used to investigate the mechanical properties of the extracellular matrix protein fibronectin. The simulations suggest that the mechanical stability of the tenth type III domain from fibronectin (FNfn10) is largely determined by a number of critical hydrogen bonds in the peripheral strands. Interestingly, the simulations predict that lowering the pH from 7 to approximately 4.7 will increase the mechanical stability of FNfn10 significantly (by approximately 33 %) due to the protonation of a few key acidic residues in the A and B strands. To test this simulation prediction, we used single-molecule atomic force microscopy (AFM) to investigate the mechanical stability of FNfn10 at neutral pH and at lower pH where these key residues have been shown to be protonated. Our AFM experimental results show no difference in the mechanical stability of FNfn10 at these different pH values. These results suggest that some simulations may overestimate the role played by electrostatic interactions in determining the mechanical stability of proteins.
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