Modulation of titin-based stiffness by disulfide bonding in the cardiac titin N2-B unique sequence.

@article{Grtzner2009ModulationOT,
  title={Modulation of titin-based stiffness by disulfide bonding in the cardiac titin N2-B unique sequence.},
  author={Anika Gr{\"u}tzner and Sergi Garcia-Manyes and Sebastian K{\"o}tter and Carmen L. Badilla and J. M. Fern{\'a}ndez and Wolfgang A Linke},
  journal={Biophysical journal},
  year={2009},
  volume={97 3},
  pages={825-34}
}
The giant protein titin is responsible for the elasticity of nonactivated muscle sarcomeres. Titin-based passive stiffness in myocardium is modulated by titin-isoform switching and protein-kinase (PK)A- or PKG-dependent titin phosphorylation. Additional modulatory effects on titin stiffness may arise from disulfide bonding under oxidant stress, as many immunoglobulin-like (Ig-)domains in titin's spring region have a potential for S-S formation. Using single-molecule atomic force microscopy (AFM… CONTINUE READING
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