Mechanical dissociation of the M-band titin/obscurin complex is directionally dependent.

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.
(Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)