ArticleThe Biochemical journal2003
Malleable conformation of the elastic PEVK segment of titin: non-co-operative interconversion of polyproline II helix, beta-turn and unordered structures.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Titin's Intrinsically Disordered PEVK Domain Modulates Actin Polymerization.International journal of molecular sciences · 2025Article
- Myofilament-associated proteins with intrinsic disorder (MAPIDs) and their resolution by computational modeling.Quarterly reviews of biophysics · 2023Review
- The titin N2B and N2A regions: biomechanical and metabolic signaling hubs in cross-striated muscles.Biophysical reviews · 2021Review
- The whole is greater than the sum of its parts: at the intersection of order, disorder, and kinetochore function.Essays in biochemistry · 2020Review
- Molecular Basis of S100A1 Activation and Target Regulation Within Physiological Cytosolic CaFrontiers in molecular biosciences · 2020Article
- The increase in non-cross-bridge forces after stretch of activated striated muscle is related to titin isoforms.American journal of physiology. Cell physiology · 2016Article
- Non-crossbridge forces in activated striated muscles: a titin dependent mechanism of regulation?Journal of muscle research and cell motility · 2015Review
- Article
- Structure of giant muscle proteins.Frontiers in physiology · 2013Review
- 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
- The mechanisms of the residual force enhancement after stretch of skeletal muscle: non-uniformity in half-sarcomeres and stiffness of titin.Proceedings. Biological sciences · 2012Review
- Conformation-regulated mechanosensory control via titin domains in cardiac muscle.Pflugers Archiv : European journal of physiology · 2011Review
- 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
- Modular structure of smooth muscle Myosin light chain kinase: hydrodynamic modeling and functional implications.Biochemistry · 2010Article
- The myofibrillar protein, projectin, is highly conserved across insect evolution except for its PEVK domain.Journal of molecular evolution · 2008Article
- Molecular and supramolecular structural studies on human tropoelastin sequences.Biophysical journal · 2007Article
- Interaction forces between F-actin and titin PEVK domain measured with optical tweezers.Biophysical journal · 2007Article
- Studies on titin PEVK peptides and their interaction.Archives of biochemistry and biophysics · 2006Article
- Hierarchical extensibility in the PEVK domain of skeletal-muscle titin.Biophysical journal · 2005Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To understand the structural basis of molecular elasticity and protein interaction of the elastic PEVK (Pro-Glu-Val-Lys) segment of the giant muscle protein titin, we carried out a detailed analysis of a representative PEVK module and a 16-module PEVK protein under various environmental conditions. Three conformational states, polyproline II (PPII) helix, beta-turn and unordered coil were identified by CD and NMR. These motifs interconvert without long-range co-operativity. As a general trend, the relative content of PPII increases with lower temperature and higher polarity, beta-turn increases with lower temperature and lower polarity, and unordered coil increases with higher temperature and higher polarity. NMR studies demonstrate that trans -proline residues are the predominant form at room temperature (22 degrees C), with little trans -to- cis isomerization below 35 degrees C. Ionic strength affects salt bridges between charged side chains, but not the backbone conformation. We conclude that titin PEVK conformation is malleable and responds to subtle environmental changes without co-operativity. This gradual conformational transition may represent a regulatory mechanism for fine-tuning protein interactions and elasticity.
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