ArticleJournal of muscle research and cell motility2005
Titin PEVK segment: charge-driven elasticity of the open and flexible polyampholyte.
Article in Journal of muscle research and cell motility, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Article
- Titin: roles in cardiac function and diseases.Frontiers in physiology · 2024Review
- Regulation of Poly-E Motif Flexibility by pH, CaInternational journal of molecular sciences · 2022Article
- Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease.Cells · 2020Review
- Molecular Basis of S100A1 Activation and Target Regulation Within Physiological Cytosolic CaFrontiers in molecular biosciences · 2020Article
- Evolution of the Highly Repetitive PEVK Region of Titin Across Mammals.G3 (Bethesda, Md.) · 2019Article
- Modulation of Disordered Proteins with a Focus on Neurodegenerative Diseases and Other Pathologies.International journal of molecular sciences · 2019Review
- Titin-based mechanosensing modulates muscle hypertrophy.Journal of cachexia, sarcopenia and muscle · 2018Article
- The Effect of Different Porogens on Porous PMMA Microspheres by Seed Swelling Polymerization and Its Application in High-Performance Liquid Chromatography.Materials (Basel, Switzerland) · 2018Article
- Phosphorylation and calcium antagonistically tune myosin-binding protein C's structure and function.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Unraveling protein-protein interactions in clathrin assemblies via atomic force spectroscopy.Methods (San Diego, Calif.) · 2013Article
- Conformational dynamics of titin PEVK explored with FRET spectroscopy.Biophysical journal · 2012Article
- Engineering of an elastic scaffolding polyprotein based on an SH3-binding intrinsically disordered titin PEVK module.Protein expression and purification · 2012Article
- Extensive and modular intrinsically disordered segments in C. elegans TTN-1 and implications in filament binding, elasticity and oblique striation.Journal of molecular biology · 2010Article
- The effects of PKCalpha phosphorylation on the extensibility of titin's PEVK element.Journal of structural biology · 2010Article
- Modular structure of smooth muscle Myosin light chain kinase: hydrodynamic modeling and functional implications.Biochemistry · 2010Article
- Nanomechanics of full-length nebulin: an elastic strain gauge in the skeletal muscle sarcomere.Langmuir : the ACS journal of surfaces and colloids · 2009Article
- The myofibrillar protein, projectin, is highly conserved across insect evolution except for its PEVK domain.Journal of molecular evolution · 2008Article
- Pulling single molecules of titin by AFM--recent advances and physiological implications.Pflugers Archiv : European journal of physiology · 2008Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The giant protein titin spans half of the sarcomere length and anchors the myosin thick filament to the Z-line of skeletal and cardiac muscles. The passive elasticity of muscle at a physiological range of stretch arises primarily from the extension of the PEVK segment, which is a polyampholyte with dense and alternating-charged clusters. Force spectroscopy studies of a 51 kDa fragment of the human fetal titin PEVK domain (TP1) revealed that when charge interactions were reduced by raising the ionic strength from 35 to 560 mM, its mean persistence length increased from 0.30 +/- 0.04 nm to 0.60 +/- 0.07 nm. In contrast, when the secondary structure of TP1 was altered drastically by the presence of 40 and 80% (v/v) of trifluoroethanol, its force-extension behavior showed no significant shift in the mean persistence length of approximately approximately 0.18 +/- 0.03 nm at the ionic strength of 15 mM. Additionally, the mean persistence length also increased from 0.29 to 0.41 nm with increasing calcium concentration from pCa 5-8 to pCa 3-4. We propose that PEVK is not a simple entropic spring as is commonly assumed, but a highly evolved, gel-like enthalpic spring with its elasticity dominated by the sequence-specific charge interactions. A single polyampholyte chain may be fine-tuned to generate a broad range of molecular elasticity by varying charge pairing schemes and chain configurations.
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Registered trials
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