✦ LIBER ✦

Mechanical properties of tropomyosin and implications for muscle regulation

✍ Scribed by George N. Phillips Jr.; Susan Chacko

Publisher: Wiley (John Wiley & Sons)
Year: 1996
Tongue: English
Weight: 664 KB
Volume: 38
Category: Article
ISSN: 0006-3525
DOI: 10.1002/(sici)1097-0282(199601)38:1<89::aid-bip7>3.0.co;2-s

No coin nor oath required. For personal study only.

✦ Synopsis

Tropomyosin is a protein that controls the interactions of actin and myosin as a part qfthe regulation of muscle contraction. The 420 A' long a-helical coiled-coil molecules form long filaments, both in muscle and in crystals. The x-ray diffraction data from tropomyosin crystals have indicated large scale motions ofthefilaments that can be related to the inherent mechanical properties ofthe molecule, and by extension, to the role oftropomyosin in the cooperative activation ofthe thin,filament.s of muscle. Diffuse scattering analysis has provided information about the amplitudes ofthe motions that has been used to calculate the intrinsic flexibility of the molecule. It can then be shown that each tropomyosin molecule by itselfcan only mediate interactions ofthe nearest-neighboring tropomyosin molecules along the filament. The repeating nature ofthe thin filament, however, allows the entire filament to activate cooperatively.

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