ArticleJournal of muscle research and cell motility2002
Unfolding of titin domains studied by molecular dynamics simulations.
Article in Journal of muscle research and cell motility, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 65 citations in OpenAlex.
- Differences in stability and calcium sensitivity of the Ig domains in titin's N2A region.Protein science : a publication of the Protein Society · 2020Article
- Monitoring Unfolding of Titin I27 Single and Bi Domain with High-Pressure NMR Spectroscopy.Biophysical journal · 2018Article
- Insights and Challenges of Multi-Scale Modeling of Sarcomere Mechanics in cTn and Tm DCM Mutants-Genotype to Cellular Phenotype.Frontiers in physiology · 2017Review
- Computing Average Passive Forces in Sarcomeres in Length-Ramp Simulations.PLoS computational biology · 2016Article
- Atomic resolution probe for allostery in the regulatory thin filament.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Molecular basis of the mechanical hierarchy in myomesin dimers for sarcomere integrity.Biophysical journal · 2014Article
- Engineering proteins with enhanced mechanical stability by force-specific sequence motifs.Proteins · 2012Article
- Article
- Interplay of mechanical and binding properties of Fibronectin type I.Theoretical chemistry accounts · 2010Article
- Tertiary and secondary structure elasticity of a six-Ig titin chain.Biophysical journal · 2010Article
- Discovery through the computational microscope.Structure (London, England : 1993) · 2009Review
- Exploration of the activation pathway of Deltaalpha-Chymotrypsin with molecular dynamics simulations and correlation with kinetic experiments.European biophysics journal : EBJ · 2008Article
- Stabilization provided by neighboring strands is critical for the mechanical stability of proteins.Biophysical journal · 2008Article
- Article
- Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of alpha-helical and beta-sheet protein domains.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Secondary and tertiary structure elasticity of titin Z1Z2 and a titin chain model.Biophysical journal · 2007Article
- Single-molecule force spectroscopy reveals a mechanically stable protein fold and the rational tuning of its mechanical stability.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- The mechanical unfolding of ubiquitin through all-atom Monte Carlo simulation with a Go-type potential.Biophysical journal · 2007Article
- Computational study of coagulation factor VIIa's affinity for phospholipid membranes.European biophysics journal : EBJ · 2007Article
- Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations.Biophysical journal · 2005Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Titin, a approximately 1 micron long protein found in striated muscle myofibrils, possesses unique elastic properties. The extensible behavior of titin has been demonstrated in atomic force microscopy and optical tweezer experiments to involve the reversible unfolding of individual immunoglobulin-like (Ig) domains. We have used steered molecular dynamics (SMD), a novel computer simulation method, to investigate the mechanical response of single titin Ig domains upon stress. Simulations of stretching Ig domains I1 and I27 have been performed in a solvent of explicit water molecules. The SMD approach provides a detailed structural and dynamic description of how Ig domains react to external forces. Validation of SMD results includes both qualitative and quantitative agreement with AFM recordings. Furthermore, combining SMD with single molecule experimental data leads to a comprehensive understanding of Ig domains' mechanical properties. A set of backbone hydrogen bonds that link the domains' terminal beta-strands play a key role in the mechanical resistance to external forces. Slight differences in architecture permit a mechanical unfolding intermediate for I27, but not for I1. Refolding simulations of I27 demonstrate a locking mechanism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.