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Mechanical dissociation of the M‐band titin/obscurin complex is directionally dependent
Author(s) -
Caldwell Tracy A.,
Sumner Isaiah,
Wright Nathan T.
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.05.023
Subject(s) - titin , obscurin , dissociation (chemistry) , chemistry , biophysics , sarcomere , microbiology and biotechnology , biology , myocyte
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.