Key result
AMP-P(NH)P enables extensive formation of a ternary acto.S-1.AMP-P(NH)P complex, with 1 mol of S-1.AMP-P(NH)P binding per mol of actin monomer without significant cooperativity.
Population
Actin, 5'-adenylyl imidodiphosphate [AMP-P(NH)P], and myosin subfragments (S-1 and HMM)
Comparison
Addition of AMP-P(NH)P vs Reaction with ATP
Design
Preclinical
Authors
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No immediate clinical implications for cardiac contractility; leaves open validation of ternary complex dynamics in mammalian models.
The study demonstrates the extensive formation of a ternary complex between actin, myosin subfragment 1, and AMP-P(NH)P, providing insights into muscle protein interactions.
Greene et al. (1978) studied this question. 5'-adenylyl imidodiphosphate [AMP-P(NH)P] vs. ATP was evaluated on Formation of the ternary complex and dissociation of actin.S-1. AMP-P(NH)P enables extensive formation of a ternary acto.S-1.AMP-P(NH)P complex, with 1 mol of S-1.AMP-P(NH)P binding per mol of actin monomer without significant cooperativity.
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