Publikation: Tertiary and secondary structure elasticity of a six-Ig titin chain
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The protein titin functions as a mechanical spring conferring passive elasticity to muscle. Force spectroscopy studies have shown that titin exhibits several regimes of elasticity. Disordered segments bring about a soft, entropic spring-type elasticity; secondary structures of titin's immunoglobulin-like (Ig-) and fibronectin type III-like (FN-III) domains provide a stiff elasticity. In this study, we demonstrate a third type of elasticity due to tertiary structure and involving domain-domain interaction and reorganization along the titin chain. Through 870 ns of molecular dynamics simulations involving 29,000-635,000 atom systems, the mechanical properties of a six-Ig domain segment of titin (I65-I70), for which a crystallographic structure is available, are probed. The results reveal a soft tertiary structure elasticity. A remarkably accurate statistical mechanical description for this elasticity is derived and applied. Simulations also studied the stiff, secondary structure elasticity of the I65-I70 chain due to the unraveling of its domains and revealed how force propagates along the chain during the secondary structure elasticity response.
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LEE, Eric H, Jen HSIN, Eleonore VON CASTELMUR, Olga MAYANS, Klaus SCHULTEN, 2010. Tertiary and secondary structure elasticity of a six-Ig titin chain. In: Biophysical journal. 2010, 98(6), pp. 1085-1095. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2009.12.4192BibTex
@article{Lee2010Terti-42009,
year={2010},
doi={10.1016/j.bpj.2009.12.4192},
title={Tertiary and secondary structure elasticity of a six-Ig titin chain},
number={6},
volume={98},
issn={0006-3495},
journal={Biophysical journal},
pages={1085--1095},
author={Lee, Eric H and Hsin, Jen and von Castelmur, Eleonore and Mayans, Olga and Schulten, Klaus}
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<dcterms:abstract xml:lang="eng">The protein titin functions as a mechanical spring conferring passive elasticity to muscle. Force spectroscopy studies have shown that titin exhibits several regimes of elasticity. Disordered segments bring about a soft, entropic spring-type elasticity; secondary structures of titin's immunoglobulin-like (Ig-) and fibronectin type III-like (FN-III) domains provide a stiff elasticity. In this study, we demonstrate a third type of elasticity due to tertiary structure and involving domain-domain interaction and reorganization along the titin chain. Through 870 ns of molecular dynamics simulations involving 29,000-635,000 atom systems, the mechanical properties of a six-Ig domain segment of titin (I65-I70), for which a crystallographic structure is available, are probed. The results reveal a soft tertiary structure elasticity. A remarkably accurate statistical mechanical description for this elasticity is derived and applied. Simulations also studied the stiff, secondary structure elasticity of the I65-I70 chain due to the unraveling of its domains and revealed how force propagates along the chain during the secondary structure elasticity response.</dcterms:abstract>
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