2026-09-18T20:13:23Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/80632 2023-07-11 col_2142_5131 col_2142_8859 com_2142_5130 com_2142_8858 com_2142_234

Aksimentiev, Aleksei Schulten, Klaus Hsin, Ya-Chieh 2015-09-25T20:03:22Z 2015-09-25T20:03:22Z 10000-01-01 2010 2010 Titin is a mechanical protein that protects muscle from overstretching by producing a restoring force when a muscle fiber is extended beyond its normal length. 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 titins immunoglobulin-like (Ig-) and fibronectin type III-like (FN-III) domains provide a stiff elasticity. We demonstrated that titin exhibits a third type of elasticity due to tertiary structure and involving domain-domain interaction and reorganization along the titin chain. Through simulations employing equilibrium molecular dynamics, steered molecular dynamics, and free-energy calculations, the mechanical properties of a six-Ig domain of titin (I65-I70), for which a crystallographic structure is available, were investigated. The results reveal a soft tertiary structure elasticity. A remarkably accurate statistical mechanical description for this elasticity is derived and applied. Simulations studied also 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. Made available in DSpace on 2015-09-25T20:03:22Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3452176.pdf: 12174376 bytes, checksum: 2b2d08b0c654db00d8e006dc26087f32 (MD5) Previous issue date: 2010 Embargo set by: Seth Robbins for item 81914 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 89 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2010. http://hdl.handle.net/2142/80632 (MiAaPQ)AAI3452176 eng Biology, Cell Computational Investigations of Cellular Functions: Three Cases on Membrane Morphogenesis, Organization and Assembly of a Multi-Protein Complex, and the Molecular Origin of Muscle Elasticity text Physics Physics University of Illinois at Urbana-Champaign Dissertation Ph.D.