ArticleBiophysical journal2002
Steered molecular dynamics studies of titin I1 domain unfolding.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Deciphering the sequence-dependent unfolding pathways of an RNA pseudoknot with steered molecular dynamics.Journal of computer-aided molecular design · 2025Article
- Mechanically weak and highly dynamic state of mechanosensitive titin Ig domains induced by proline isomerization.Nature communications · 2025Article
- The α-Synuclein Monomer May Have Different Misfolding Mechanisms in the Induction of α-Synuclein Fibrils with Different Polymorphs.Biomolecules · 2023Article
- Assessing the Stability of Biological Fibrils by Molecular-Scale Simulations.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Microbial production of megadalton titin yields fibers with advantageous mechanical properties.Nature communications · 2021Article
- Neuropilin-1 assists SARS-CoV-2 infection by stimulating the separation of Spike protein S1 and S2.Biophysical journal · 2021Article
- Impact of an alpha helix and a cysteine-cysteine disulfide bond on the resistance of bacterial adhesion pili to stress.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Neuropilin-1 Assists SARS-CoV-2 Infection by Stimulating the Separation of Spike Protein Domains S1 and S2.bioRxiv : the preprint server for biology · 2021Article
- The Poly-E motif in Titin's PEVK region undergoes pH dependent conformational changes.Biochemistry and biophysics reports · 2020Article
- Differences in stability and calcium sensitivity of the Ig domains in titin's N2A region.Protein science : a publication of the Protein Society · 2020Article
- Protein unfolding by SDS: the microscopic mechanisms and the properties of the SDS-protein assembly.Nanoscale · 2020Article
- Obscurin is a semi-flexible molecule in solution.Protein science : a publication of the Protein Society · 2019Article
- Differences in the mechanical unfolding pathways of apo- and copper-bound azurins.Scientific reports · 2018Article
- The influence of disulfide bonds on the mechanical stability of proteins is context dependent.The Journal of biological chemistry · 2017Article
- Effects of ligand binding on the mechanical stability of protein GB1 studied by steered molecular dynamics simulation.Journal of molecular modeling · 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
- Interrogating the activities of conformational deformed enzyme by single-molecule fluorescence-magnetic tweezers microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A computational model of the glycine tautomerization reaction in aqueous solution.Journal of molecular modeling · 2014Article
- Single-molecule studies on PolySUMO proteins reveal their mechanical flexibility.Biophysical journal · 2013Article
- Membrane-induced lever arm expansion allows myosin VI to walk with large and variable step sizes.The Journal of biological chemistry · 2012Article
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3 authors.
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Abstract
The cardiac muscle protein titin, responsible for developing passive elasticity and extensibility of muscle, possesses about 40 immunoglobulin-like (Ig) domains in its I-band region. Atomic force microscopy (AFM) and steered molecular dynamics (SMD) have been successfully combined to investigate the reversible unfolding of individual Ig domains. However, previous SMD studies of titin I-band modules have been restricted to I27, the only structurally known Ig domain from the distal region of the titin I-band. In this paper we report SMD simulations unfolding I1, the first structurally available Ig domain from the proximal region of the titin I-band. The simulations are carried out with a view toward upcoming atomic force microscopy experiments. Both constant velocity and constant force stretching have been employed to model mechanical unfolding of oxidized I1, which has a disulfide bond bridging beta-strands C and E, as well as reduced I1, in which the disulfide bridge is absent. The simulations reveal that I1 is protected against external stress mainly through six interstrand hydrogen bonds between its A and B beta-strands. The disulfide bond enhances the mechanical stability of oxidized I1 domains by restricting the rupture of backbone hydrogen bonds between the A'- and G-strands. The disulfide bond also limits the maximum extension of I1 to approximately 220 A. Comparison of the unfolding pathways of I1 and I27 are provided and implications to AFM experiments are discussed.
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