ArticleBiophysical journal2000
The key event in force-induced unfolding of Titin's immunoglobulin domains.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.
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Who cites it
95 citing papers in PubMed.
- Single-Molecule Force Spectroscopy: Experiments, Analysis, and Simulations.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Computational design of superstable proteins through maximized hydrogen bonding.Nature chemistry · 2026Article
- PySteMoDA: An Open-Source Python Package for the Analysis of Steered Molecular Dynamics Simulations Data.bioRxiv : the preprint server for biology · 2026Article
- The local mechanostructural properties of protein cargoes regulate nucleocytoplasmic transport.Nature physics · 2026Article
- Conformational response of αStructure (London, England : 1993) · 2025Article
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- Structural anisotropy results in mechano-directional transport of proteins across nuclear pores.Nature physics · 2024Article
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
- Exploring the Effect of Mechanical Anisotropy of Protein Structures in the Unfoldase Mechanism of AAA+ Molecular Machines.Nanomaterials (Basel, Switzerland) · 2022Article
- Contribution of hydrophobic interactions to protein mechanical stability.Computational and structural biotechnology journal · 2022Article
- Piecewise All-Atom SMD Simulations Reveal Key Secondary Structures in Luciferase Unfolding Pathway.Biophysical journal · 2020Article
- Protein unfolding by SDS: the microscopic mechanisms and the properties of the SDS-protein assembly.Nanoscale · 2020Article
- Article
- Heterogeneous and rate-dependent streptavidin-biotin unbinding revealed by high-speed force spectroscopy and atomistic simulations.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Monitoring Unfolding of Titin I27 Single and Bi Domain with High-Pressure NMR Spectroscopy.Biophysical journal · 2018Article
- Molecular mechanism of extreme mechanostability in a pathogen adhesin.Science (New York, N.Y.) · 2018Article
- Force generation by titin folding.Protein science : a publication of the Protein Society · 2017Article
- Nanomechanical properties of MscL α helices: A steered molecular dynamics study.Channels (Austin, Tex.) · 2017Article
- Modeling the human NaDrug design, development and therapy · 2017Article
- Native flexibility of structurally homologous proteins: insights from anisotropic network model.BMC biophysics · 2017Article
35 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors.
Funding
Abstract
Steered molecular dynamics simulation of force-induced titin immunoglobulin domain I27 unfolding led to the discovery of a significant potential energy barrier at an extension of approximately 14 A on the unfolding pathway that protects the domain against stretching. Previous simulations showed that this barrier is due to the concurrent breaking of six interstrand hydrogen bonds (H-bonds) between beta-strands A' and G that is preceded by the breaking of two to three hydrogen bonds between strands A and B, the latter leading to an unfolding intermediate. The simulation results are supported by Angstrom-resolution atomic force microscopy data. Here we perform a structural and energetic analysis of the H-bonds breaking. It is confirmed that H-bonds between strands A and B break rapidly. However, the breaking of the H-bond between strands A' and G needs to be assisted by fluctuations of water molecules. In nanosecond simulations, water molecules are found to repeatedly interact with the protein backbone atoms, weakening individual interstrand H-bonds until all six A'-G H-bonds break simultaneously under the influence of external stretching forces. Only when those bonds are broken can the generic unfolding take place, which involves hydrophobic interactions of the protein core and exerts weaker resistance against stretching than the key event.
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