Biophysical Reviews

, Volume 3, Issue 4, pp 199–207

Mechanisms of residual force enhancement in skeletal muscle: insights from experiments and mathematical models


DOI: 10.1007/s12551-011-0059-2

Cite this article as:
Campbell, S.G. & Campbell, K.S. Biophys Rev (2011) 3: 199. doi:10.1007/s12551-011-0059-2


A skeletal muscle that is stretched while contracting will produce more force at steady state than if it is stretched passively and then stimulated to contract. This phenomenon is known as residual force enhancement and has been widely studied since its description more than 60 years ago. The idea that the mechanical properties of a muscle are governed not just by its present length but also by its length at earlier time points has far reaching implications since muscles stretch and shorten routinely in normal use. In this review, we present the experimental and theoretical advances that have been made toward understanding the mechanisms that underlie residual force enhancement. In the past 10 years, experiments and models have focused on essentially three candidate mechanisms for residual force enhancement: (half-) sarcomere inhomogeneity, activity of so-called ‘passive’ mechanical elements in the sarcomere (titin), and the intrinsic properties of myosin crossbridges. Evidence, both computational and experimental, is accumulating for each of these mechanisms such that a final description of the phenomenon seems attainable in the near future. We conclude that computational models that incorporate more than one putative mechanism may ultimately facilitate reconciliation of the growing number of ideas and experimental data in this field.


Residual force enhancementComputational modelingSkeletal muscleHalf-sarcomeres

Copyright information

© International Union for Pure and Applied Biophysics (IUPAB) and Springer 2011

Authors and Affiliations

  1. 1.Department of Physiology and Center for Muscle BiologyUniversity of KentuckyLexingtonUSA
  2. 2.Department of PhysiologyMS508 Chandler Medical CenterLexingtonUSA