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- W2790072995 abstract "Human cardiac myosin has two isoforms, alpha and beta, coexisting in healthy muscle. These isoforms share significant sequence similarity, but they are different in kinetics: ADP release from actomyosin is an order of magnitude faster in alpha myosin isoform. Apparently, small differences in sequence are responsible for distinct local inter-residue interactions within alpha and beta isoforms, leading to particular rate of ADP release. Previously we analyzed structural differences of alpha and beta isoforms with molecular dynamics simulations, and found several places within myosin head with distinct dynamics of local structural elements. We hypothesize that isoform-specific electrostatic interactions play a role in that difference. In this work we examined one of those places within myosin head, the force-generation region, and particularly helix SH1. According to our simulations, the helix experiences helix-loop transition in alpha isoform. Our analysis shows that, within the force-generating region, R694 displays one of the most marked differences between isoforms. In beta isoform, this residue forms two permanent salt bridges, which are not present in alpha isoform. We prepared R694N mutant of beta isoform of human cardiac myosin to destabilize two salt bridges in the force-generating region. The mutant supports ATPase activity. We report on the kinetics of ADP release from actomyosin with and without mutation, and conclude on the role of electrostatic interactions within the force-generating region on the kinetics of ADP release from actomyosin." @default.
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- W2790072995 date "2018-02-01" @default.
- W2790072995 modified "2023-09-30" @default.
- W2790072995 title "Role of Electrostatic Interactions in the Isoform-Specific Rate of ADP Release from Human Cardiac Myosin" @default.
- W2790072995 doi "https://doi.org/10.1016/j.bpj.2017.11.791" @default.
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