ArticleBiophysical journal2009
The effect of different force applications on the protein-protein complex Barnase-Barstar.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Computational screening of the effects of mutations on protein-protein off-rates and dissociation mechanisms by τRAMD.Communications biology · 2024Article
- Protein-Protein Binding as a Two-Step Mechanism: Preselection of Encounter Poses during the Binding of BPTI and Trypsin.Biophysical journal · 2020Article
- Protein Interaction with Charged Macromolecules: From Model Polymers to Unfolded Proteins and Post-Translational Modifications.International journal of molecular sciences · 2019Review
- Energy landscape of all-atom protein-protein interactions revealed by multiscale enhanced sampling.PLoS computational biology · 2014Article
- Strength of hydrogen bond network takes crucial roles in the dissociation process of inhibitors from the HIV-1 protease binding pocket.PloS one · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Steered molecular dynamics simulations are a tool to examine the energy landscape of protein-protein complexes by applying external forces. Here, we analyze the influence of the velocity and geometry of the probing forces on a protein complex using this tool. With steered molecular dynamics, we probe the stability of the protein-protein complex Barnase-Barstar. The individual proteins are mechanically labile. The Barnase-Barstar binding site is more stable than the folds of the individual proteins. By using different force protocols, we observe a variety of responses of the system to the applied tension.
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