ArticleBiophysical journal2004
Origin of mechanical strength of bovine carbonic anhydrase studied by molecular dynamics simulation.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Conservation of knotted and slipknotted topology in transmembrane transporters.Biophysical journal · 2023Article
- In Silico Designing of an Industrially Sustainable Carbonic Anhydrase Using Molecular Dynamics Simulation.ACS omega · 2016Article
- Conservation of complex knotting and slipknotting patterns in proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Identification of a mechanical rheostat in the hydrophobic core of protein L.Journal of molecular biology · 2009Article
- Exploring local flexibility/rigidity in psychrophilic and mesophilic carbonic anhydrases.Biophysical journal · 2009Article
- Tensile mechanics of alanine-based helical polypeptide: force spectroscopy versus computer simulations.Biophysical journal · 2009Article
- Stochastic emergence of multiple intermediates detected by single-molecule quasi-static mechanical unfolding of protein.Biophysics (Nagoya-shi, Japan) · 2009Article
- Nanobiomechanics of proteins and biomembrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2008Article
- Competitive inhibitory effects of acetazolamide upon interactions with bovine carbonic anhydrase II.The protein journal · 2007Article
- Characterizing folding, structure, molecular interactions and ligand gated activation of single sodium/proton antiporters.Naunyn-Schmiedeberg's archives of pharmacology · 2006Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The forced unfolding process of bovine carbonic anhydrase II (BCA II) was examined at the atomic level by the molecular dynamics (MD) simulation. By force spectroscopy, experimentally obtained force-extension curves (F-E curves) showed a prominent force peak after 50 nm extension. F-E curves obtained from our simulation had three force peaks appearing after extensions of 10-17 nm, 40 nm, and 53 nm, each signifying a brittle fracture of a specific local structure. Upon undergoing the final fracture at 53 nm of extension, the entire molecule became a single flexible chain and was further extended to its full theoretical length, almost as a random coil. This feature of the 53-nm peak strongly suggested its close correspondence to the experimentally observed force peak at approximately 60-nm extension. The 53-nm peak in the molecular dynamics simulation corresponded to the unfolding process of the beta-sheeted core that includes zinc-coordinating histidine residues. These results suggest that the structural change occurring at 50-60 nm in atomic force microscopy experiments corresponded to the destruction of the zinc coordination site.
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