A combined experimental and computational analysis of mantATP turnover in skinned muscle fibers.

ABSTRACT: Myosin is the primary motor protein in skeletal muscle, responsible for adenosine triphosphate (ATP) hydrolysis that drives muscle contraction. In addition to force production, resting myosin consumes ATP in futile cycles at two rates, the slower one being associated with the Super Relaxed State (SRX), in contrast to the less inhibited Disordered Relaxed State (DRX). The SRX is typically measured using the mantATP chasing technique, where the decay of a fluorescent ATP analogue is fitted using a multiexponential function. Recently, significant concerns have been raised regarding the use of this technique, particularly when applied to soluble myosin preparations. While skinned fibers offer the advantage of preserving the native thick filament structure and myosin cooperativity, limited diff

SUBMITTER: Montesel M 

PROVIDER: S-EPMC12107101 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature