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Tertiary and Secondary Structure Elasticity of a Six-Ig Titin Chain
Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois; Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, Illinois; College of Medicine, University of Illinois at Urbana-Champaign, Urbana, Illinois.
Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, Illinois; Department of Physics, University of Illinois at Urbana-Champaign, Urbana, Illinois.
School of Biological Sciences, University of Liverpool, Liverpool, United Kingdom.
School of Biological Sciences, University of Liverpool, Liverpool, United Kingdom.
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2010 (English)In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 98, no 6, p. 1085-1095Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
St. Louis, MO, United States: Cell Press , 2010. Vol. 98, no 6, p. 1085-1095
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:liu:diva-143667DOI: 10.1016/j.bpj.2009.12.4192ISI: 000275842200022PubMedID: 20303866Scopus ID: 2-s2.0-77949648622OAI: oai:DiVA.org:liu-143667DiVA: diva2:1165126
Available from: 2017-12-12 Created: 2017-12-12 Last updated: 2017-12-21Bibliographically approved

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von Castelmur, Eleonore

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