Tropomyosin pp 60-72 | Cite as

Tropomyosin: Function Follows Structure

  • Sarah E. Hitchcock-DeGregori
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 644)


Tropomyosin is known as the archetypal coiled coil, being the first to be sequenced and modeled. Studies of the structure and dynamics of tropomyosin, accompanied by biochemical and biophysical analyses of tropomyosin, mutants and model peptides, have revealed the complexity and subtleties required for tropomyosin function. Interruptions in the canonical coiled coil allow for bends and regions of local instability that are required for tropomyosin to bind to the helical actin filament. This chapter highlights insights gained from recent structural studies as they relate to variations in tropomyosin’s coiled-coil structure that are essential for binding to actin and the relationship of periodic repeats to actin molecules in the filament.


Coiled Coil Actin Binding Interface Residue Actin Monomer RCSB Protein Data 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Landes Bioscience and Springer Science+Business Media 2008

Authors and Affiliations

  • Sarah E. Hitchcock-DeGregori
    • 1
  1. 1.Department of Neuroscience and Cell BiologyRobert Wood Johnson Medical SchoolPiscatawayUSA

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