Key result
Tropomyosin abolished the cross-link between the central 48-kDa fragment of the S1 heavy chain and Lys50 of actin subdomain 2, preventing the formation of the 200-kDa acto-S1 complex.
Tropomyosin alters the structure of actin subdomain 2 and inhibits specific cross-linking with the myosin head, providing insight into the weak acto-S1 binding state.
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Refines models of weak acto-S1 binding; leaves open relevance to human cardiac thin filament regulation.
Bonafé et al. (1994) studied this question. Tropomyosin vs. Absence of regulatory proteins was evaluated on Glutaraldehyde-induced cross-linking of the F-actin-myosin head (S1) complex. Tropomyosin abolished the cross-link between the central 48-kDa fragment of the S1 heavy chain and Lys50 of actin subdomain 2, preventing the formation of the 200-kDa acto-S1 complex.
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