Electron microscopy and persistence length analysis of semi-rigid smooth muscle tropomyosin strands.

@article{Sousa2010ElectronMA,
  title={Electron microscopy and persistence length analysis of semi-rigid smooth muscle tropomyosin strands.},
  author={Duncan R. Sousa and Anthony Cammarato and Ken Jang and Philip Graceffa and Larry S. Tobacman and Xiaochuan Edward Li and William Lehman},
  journal={Biophysical journal},
  year={2010},
  volume={99 3},
  pages={862-8}
}
The structural mechanics of tropomyosin are essential determinants of its affinity and positioning on F-actin. Thus, tissue-specific differences among tropomyosin isoforms may influence both access of actin-binding proteins along the actin filaments and the cooperativity of actin-myosin interactions. Here, 40 nm long smooth and striated muscle tropomyosin molecules were rotary-shadowed and compared by means of electron microscopy. Electron microscopy shows that striated muscle tropomyosin… CONTINUE READING

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