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Reverse engineering of the giant muscle protein titin

Author

Listed:
  • Hongbin Li

    (Mayo Foundation)

  • Wolfgang A. Linke

    (University of Heidelberg)

  • Andres F. Oberhauser

    (Mayo Foundation)

  • Mariano Carrion-Vazquez

    (Mayo Foundation)

  • Jason G. Kerkvliet

    (Mayo Foundation)

  • Hui Lu

    (Donald Danforth Plant Science Center)

  • Piotr E. Marszalek

    (Mayo Foundation)

  • Julio M. Fernandez

    (Mayo Foundation)

Abstract

Through the study of single molecules it has become possible to explain the function of many of the complex molecular assemblies found in cells1,2,3,4,5. The protein titin provides muscle with its passive elasticity. Each titin molecule extends over half a sarcomere, and its extensibility has been studied both in situ6,7,8,9,10 and at the level of single molecules11,12,13,14. These studies suggested that titin is not a simple entropic spring but has a complex structure-dependent elasticity. Here we use protein engineering and single-molecule atomic force microscopy15 to examine the mechanical components that form the elastic region of human cardiac titin16,17. We show that when these mechanical elements are combined, they explain the macroscopic behaviour of titin in intact muscle6. Our studies show the functional reconstitution of a protein from the sum of its parts.

Suggested Citation

  • Hongbin Li & Wolfgang A. Linke & Andres F. Oberhauser & Mariano Carrion-Vazquez & Jason G. Kerkvliet & Hui Lu & Piotr E. Marszalek & Julio M. Fernandez, 2002. "Reverse engineering of the giant muscle protein titin," Nature, Nature, vol. 418(6901), pages 998-1002, August.
    • Handle: RePEc:nat:nature:v:418:y:2002:i:6901:d:10.1038_nature00938
    DOI: 10.1038/nature00938
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    Cited by:

    1. Gudrun Schappacher-Tilp & Timothy Leonard & Gertrud Desch & Walter Herzog, 2015. "A Novel Three-Filament Model of Force Generation in Eccentric Contraction of Skeletal Muscles," PLOS ONE, Public Library of Science, vol. 10(3), pages 1-16, March.
    2. Zhongjie Ye & Nicola Galvanetto & Leonardo Puppulin & Simone Pifferi & Holger Flechsig & Melanie Arndt & Cesar Adolfo Sánchez Triviño & Michael Palma & Shifeng Guo & Horst Vogel & Anna Menini & Clemen, 2024. "Structural heterogeneity of the ion and lipid channel TMEM16F," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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