Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering.

@article{Fowler2002MechanicalUO,
  title={Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering.},
  author={Susan B. Fowler and Robert B. Best and Jos{\'e} Luis Toca Herrera and Trevor J. Rutherford and Annette Steward and Emanuele Paci and Martin Karplus and Jane Clarke},
  journal={Journal of molecular biology},
  year={2002},
  volume={322 4},
  pages={841-9}
}
The mechanical unfolding of an immunoglobulin domain from the human muscle protein titin (TI I27) has been shown to proceed via a metastable intermediate in which the A-strand is detached. The structure and properties of this intermediate are characterised in this study. A conservative destabilising mutation in the A-strand has no effect on the unfolding force, nor the dependence of the unfolding force on the pulling speed, indicating that the unfolding forces measured in an AFM experiment are… CONTINUE READING

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