ArticleBiophysical journal2007
Secondary and tertiary structure elasticity of titin Z1Z2 and a titin chain model.
Article in Biophysical journal, 2007. 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, 53 citations in OpenAlex.
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- The ZT Biopolymer: A Self-Assembling Protein Scaffold for Stem Cell Applications.International journal of molecular sciences · 2019Review
- The Assembling and Contraction Mechanisms of Striated Muscles.Frontiers in chemistry · 2018Article
- Physical characterization of nanoparticle size and surface modification using particle scattering diffusometry.Biomicrofluidics · 2016Article
- Molecular investigations into the mechanics of a muscle anchoring complex.Biophysical journal · 2015Article
- The adaptive biasing force method: everything you always wanted to know but were afraid to ask.The journal of physical chemistry. B · 2015Article
- Structure of giant muscle proteins.Frontiers in physiology · 2013Review
- An energetic model for macromolecules unfolding in stretching experiments.Journal of the Royal Society, Interface · 2013Article
- A comparative study of ribosomal proteins: linkage between amino acid distribution and ribosomal assembly.BMC biophysics · 2013Article
- Improved resolution of tertiary structure elasticity in muscle protein.Biophysical journal · 2011Article
- 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
- Exploring Multidimensional Free Energy Landscapes Using Time-Dependent Biases on Collective Variables.Journal of chemical theory and computation · 2010Article
- Beyond lamins other structural components of the nucleoskeleton.Methods in cell biology · 2010Review
- Dynamic strength of titin's Z-disk end.Journal of biomedicine & biotechnology · 2010Article
- Discovery through the computational microscope.Structure (London, England : 1993) · 2009Review
- Elasticity and rupture of a multi-domain neural cell adhesion molecule complex.Biophysical journal · 2009Article
- The myofibrillar protein, projectin, is highly conserved across insect evolution except for its PEVK domain.Journal of molecular evolution · 2008Article
- The allosteric role of the Ca2+ switch in adhesion and elasticity of C-cadherin.Biophysical journal · 2008Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The giant protein titin, which is responsible for passive elasticity in muscle fibers, is built from approximately 300 regular immunoglobulin-like (Ig) domains and FN-III repeats. While the soft elasticity derived from its entropic regions, as well as the stiff mechanical resistance derived from the unfolding of the secondary structure elements of Ig- and FN-III domains have been studied extensively, less is known about the mechanical elasticity stemming from the orientation of neighboring domains relative to each other. Here we address the dynamics and energetics of interdomain arrangement of two adjacent Ig-domains of titin, Z1, and Z2, using molecular dynamics (MD) simulations. The simulations reveal conformational flexibility, due to the domain-domain geometry, that lends an intermediate force elasticity to titin. We employ adaptive biasing force MD simulations to calculate the energy required to bend the Z1Z2 tandem open to identify energetically feasible interdomain arrangements of the Z1 and Z2 domains. The finding is cast into a stochastic model for Z1Z2 interdomain elasticity that is generalized to a multiple domain chain replicating many Z1Z2-like units and representing a long titin segment. The elastic properties of this chain suggest that titin derives so-called tertiary structure elasticity from bending and twisting of its domains. Finally, we employ steered molecular dynamics simulations to stretch individual Z1 and Z2 domains and characterize the so-called secondary structure elasticity of the two domains. Our study suggests that titin's overall elastic response at weak force stems from a soft entropic spring behavior (not described here), from tertiary structure elasticity with an elastic spring constant of approximately 0.001-1 pN/A and, at strong forces, from secondary structure elasticity.
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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.