Journal
ANNUAL REVIEW OF BIOPHYSICS, VOL 40
Volume 40, Issue -, Pages 187-203Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biophys-072110-125325
Keywords
molecular dynamics; steered molecular dynamics; elastic protein; mechanical protein
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Funding
- NCRR NIH HHS [P41-RR005969, P41 RR005969] Funding Source: Medline
- NIGMS NIH HHS [R01 GM073655] Funding Source: Medline
- NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR005969] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM073655] Funding Source: NIH RePORTER
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This review uses the giant muscle protein titin as an example to showcase the capability of molecular dynamics simulations. Titin is responsible for the passive elasticity in muscle and is a chain composed of immunoglobulin (Ig)-like and fibronectin III (FN-III)-like domains, as well as PEVK segments rich in proline (P), glutamate (E), valine (V), and lysine (K). The elasticity of titin is derived in stages of extension under increasing external force: Ig domain straightening occurs first (termed tertiary structure elasticity), followed by the extension of the disordered PEVK segments. At larger extension and force, Ig domains unfold one by one (termed secondary structure elasticity). With the availability of crystal structures of single and connected Ig domains, the tertiary and secondary structure elasticity of titin was investigated through molecular dynamics simulations, unveiling the molecular origin of titin's elasticity.
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