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Updated: Aug 18, 2026

MultiBac System-Based Purification and Biophysical Characterization of Human Myosin-7a
Published on: August 23, 2024
Myosin heavy chain isoform expression and in vivo isometric performance: a regression model
Brian K Schilling1, Andrew C Fry, Loren Z F Chiu
1Human Performance Laboratories, The University of Memphis, Memphis, Tennessee 38152, USA. bschllng@memphis.edu
Abstract:
This investigation estimated the amount of variance in voluntary in vivo muscle performance that can be explained by relative myosin heavy chain (MHC) isoform expression. The role of the relative expression of these proteins in relation to in vitro force and velocity performance is well understood, but the in vivo model is less clear. Twenty-two men and women (mean +/- SD age, 27 +/- 6 years) performed isometric knee extensor actions in which peak force and rate of force development (RFD) were measured. The results of regression analysis showed that the inclusion of MHC IIb explained a significant (19.9%, p < 0.05) amount of variance in relative peak force (adjusted for muscle mass) and 14.1% of the variance in the first half of the rise phase of the force-time curve (RFD(0-50%)) (p < 0.1). The addition of MHC I into this model explained a significant (p < 0.05) amount of variance above that accounted for by MHC IIb in RFD (45.4%), RFD(0-50%) (50.8%), and RFD(50-100%) (second half of the rise phase of the force-time curve) (37.4%). Since the percentage of MHC IIb is reduced rather quickly with training, these data suggest that peak force may also be affected quickly by training. The percentage of MHC I has a longer course for change with training; therefore, it may be inferred that the greatest changes in RFD variables will likely occur during a longer course.
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