title: Mechanical dissociation of the M-band titin/obscurin complex is directionally dependent.
abstract: Titin and obscurin, two giant muscle proteins, bind to each other in an antiparallel Ig-Ig fashion at the M-band. This interaction must be able to withstand the mechanical strain that the M-band typically experiences and remain intact. The mechanical force on these domains is likely exerted along one of two axes: a longitudinal axis, resulting in a 'shearing' force, or a lateral axis, resulting in a 'peeling' force. Here we present molecular dynamics data suggesting that these forces result in distinct unraveling pathways of the titin/obscurin complex and that peeling the domains apart requires less work and force.
authors.affiliation: Department of Chemistry and Biochemistry, James Madison University, 901 Carrier Dr., Harrisonburg, VA 22807, United States.
authors.forename: Tracy A
authors.initials: TA
authors.lastname: Caldwell
authors.affiliation: Department of Chemistry and Biochemistry, James Madison University, 901 Carrier Dr., Harrisonburg, VA 22807, United States.
authors.forename: Isaiah
authors.initials: I
authors.lastname: Sumner
authors.affiliation: Department of Chemistry and Biochemistry, James Madison University, 901 Carrier Dr., Harrisonburg, VA 22807, United States. Electronic address: wrightnt@jmu.edu.
authors.forename: Nathan T
authors.initials: NT
authors.lastname: Wright
mesh_terms: D064211:Connectin / Q000737:chemistry*; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D056004:Molecular Dynamics Simulation; D009124:Muscle Proteins / Q000737:chemistry*
chemical_list: D064211:Connectin; D009124:Muscle Proteins
keywords: M10; Muscular dystrophy; Peeling; Shearing; Steered molecular dynamic