Probing actin-activated ATP turnover kinetics of human cardiac myosin II by single molecule fluorescence.

ABSTRACT: Mechanistic insights into myosin II energy transduction in striated muscle in health and disease would benefit from functional studies of a wide range of point-mutants. This approach is, however, hampered by the slow turnaround of myosin II expression that usually relies on adenoviruses for gene transfer. A recently developed virus-free method is more time effective but would yield too small amounts of myosin for standard biochemical analyses. However, if the fluorescent adenosine triphosphate (ATP) and single molecule (sm) total internal reflection fluorescence microscopy previously used to analyze basal ATP turnover by myosin alone, can be expanded to actin-activated ATP turnover, it would appreciably reduce the required amount of myosin. To that end, we here describe zero-length cross-l

SUBMITTER: Berg A 

PROVIDER: S-EPMC11615843 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature