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Force-spectroscopy of single proteins

This study explores the mechanics of the giant muscle protein titin using force-spectroscopy techniques. We provide a detailed analysis of titin's elasticity, examining its structural properties through electron micrographs and modeling. The research highlights the mechanical design of titin and its significance in muscle function, as well as the extracellular matrix's role in cellular activity. We also discuss the implications of creating titin phenotypes in mice and the importance of fibronectin in maintaining cell adhesion within biological systems.

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Force-spectroscopy of single proteins

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  1. Force-spectroscopy of single proteins II: mechanical engineering in biological systems

  2. Igor Demonstration of analysis with models of polymer elasticity

  3. Reverse Engineering of the giant muscle protein titin

  4. The elastic protein titin is the third filament of muscle

  5. Electron micrographs of isolated titin molecules

  6. Machina Carnis

  7. Titin: a complex mechanical protein A B C D Adapted from Linke, 2007, Cardiovascular Research (in press)

  8. Measuring the extensibility of titin in a single isolated cardiac fiber

  9. Elasticity of PEVK

  10. Electron micrographs of PEVK_I27 polyprotein

  11. Persistence length of PEVK

  12. Elasticity of N2B

  13. V11P V15P V13P wt Y9P

  14. Understand the mechanical design of titin in humans Understand the molecular design of its modules Create titin phenotypes in mice

  15. Mechanical design of the extracellular matrix:fibronectin

  16. A complex web of proteins and polysaccharides that provides the mechanical scaffold for organs and tissues ECM cell membrane

  17. Fibronectin: a major, cell binding component of the ECM NMR structure of 10F3. The RGD residues are identified in the picture.

  18. Fluorescently labeled fibronectin assembled by CHO cells

  19. Mechanical unfolding of protein domains helps to keep the cells mechanically bonded. Mechanical hierarchies define the triggers of cellular activity Cell binding cryptic binding cryptic binding

  20. Mechanical design of the extracellular matrix:polysaccharides

  21. Polysaccharides cellulose amylose

  22. 0.55 nm 0.45 nm If we mechanically stretch a sugar ring, it gets longer by switching from a chair to a boat conformation

  23. Periodate oxidation cleaves the rings of pectin

  24. Ubiquitin chains form a mechanical signallingsystem in cells

  25. From Weissman, Nature Reviews, 2001, 2:169-178

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