ArticleBiophysical journal2011
Velocity-dependent mechanical unfolding of bacteriorhodopsin is governed by a dynamic interaction network.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- Factors That Control the Force Needed to Unfold a Membrane Protein in Silico Depend on the Mode of Denaturation.International journal of molecular sciences · 2023Article
- Biological physics by high-speed atomic force microscopy.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2020Review
- Piecewise All-Atom SMD Simulations Reveal Key Secondary Structures in Luciferase Unfolding Pathway.Biophysical journal · 2020Article
- Membrane-Protein Unfolding Intermediates Detected with Enhanced Precision Using a Zigzag Force Ramp.Biophysical journal · 2020Article
- On the Interpretation of Force-Induced Unfolding Studies of Membrane Proteins Using Fast Simulations.Biophysical journal · 2019Article
- Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins.Science (New York, N.Y.) · 2017Article
- Forced Unfolding Mechanism of Bacteriorhodopsin as Revealed by Coarse-Grained Molecular Dynamics.Biophysical journal · 2016Article
- YidC assists the stepwise and stochastic folding of membrane proteins.Nature chemical biology · 2016Article
- Substrate-induced changes in the structural properties of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Locating an extracellular K+-dependent interaction site that modulates betaine-binding of the Na+-coupled betaine symporter BetP.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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2 authors.
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Abstract
Bacteriorhodopsin is a model system for membrane proteins. This seven transmembrane helical protein is embedded within a membrane structure called purple membrane. Its structural stability against mechanical stress was recently investigated by atomic force microscopy experiments, in which single proteins were extracted from the purple membrane. Here, we study this process by all-atom molecular dynamics simulations, in which single bacteriorhodopsin molecules were extracted and unfolded from an atomistic purple membrane model. In our simulations, key features from the experiments like force profiles and location of key residues that resist mechanical unfolding were reproduced. These key residues were seen to be stabilized by a dynamic network of intramolecular interactions. Further, the unfolding pathway was found to be velocity-dependent. Simulations in which the mechanical stress was released during unfolding revealed relaxation motions that allowed characterization of the nonequilibrium processes during fast extraction.
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