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Tertiary and Secondary Structure Elasticity of a Six-Ig Titin Chain

Lee, Eric H (author)
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
Hsin, Jen (author)
Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, Illinois; Department of Physics, University of Illinois at Urbana-Champaign, Urbana, Illinois
von Castelmur, Eleonore (author)
School of Biological Sciences, University of Liverpool, Liverpool, United Kingdom
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Mayans, Olga (author)
School of Biological Sciences, University of Liverpool, Liverpool, United Kingdom
Schulten, Klaus (author)
Center for Biophysics and Computational Biology, 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, IllinoisN
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St. Louis, MO, United States : Cell Press, 2010
2010
English.
In: Biophysical Journal. - St. Louis, MO, United States : Cell Press. - 0006-3495 .- 1542-0086. ; 98:6, s. 1085-1095
  • Journal article (peer-reviewed)
Abstract Subject headings
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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.

Subject headings

NATURVETENSKAP  -- Kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences (hsv//eng)

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Lee, Eric H
Hsin, Jen
von Castelmur, E ...
Mayans, Olga
Schulten, Klaus
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NATURAL SCIENCES
NATURAL SCIENCES
and Chemical Science ...
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Biophysical Jour ...
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Linköping University

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