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A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
Author(s) -
Gautel Mathias,
Goulding David
Publication year - 1996
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 - 10.1016/0014-5793(96)00338-9
Subject(s) - titin , elasticity (physics) , series (stratigraphy) , obscurin , chemistry , biophysics , biology , materials science , microbiology and biotechnology , sarcomere , composite material , myocyte , paleontology
In the I‐band of skeletal muscle sarcomeres, the elastic region of titin consists of immunoglobulin (1g) domains, and non‐modular regions rich in proline, hydrophobic, and charged residues (PEVK). Using immunoelectron microscopy with sequence‐assigned monoclonal antibodies, we demonstrate that extension of the Ig regions in M. psoas occurs largely at sarcomere lengths between 2 and 2.8 μm, decreasing in slope towards higher lengths. The Ig domains do not unfold. Above 2.6 μm, length changes are increasingly due to the PEVK‐rich regions. We therefore propose that rubber‐like properties of the PEVK‐rich regions are mainly contributing to skeletal titin elasticity.