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© Research
Publication : Nature communications

Harmonic force spectroscopy measures load-dependent kinetics of individual human β-cardiac myosin molecules

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature communications - 04 Aug 2015

Sung J, Nag S, Mortensen KI, Vestergaard CL, Sutton S, Ruppel K, Flyvbjerg H, Spudich JA

Link to Pubmed [PMID] – 26239258

Nat Commun 2015 Aug;6:7931

Molecular motors are responsible for numerous cellular processes from cargo transport to heart contraction. Their interactions with other cellular components are often transient and exhibit kinetics that depend on load. Here, we measure such interactions using ‘harmonic force spectroscopy’. In this method, harmonic oscillation of the sample stage of a laser trap immediately, automatically and randomly applies sinusoidally varying loads to a single motor molecule interacting with a single track along which it moves. The experimental protocol and the data analysis are simple, fast and efficient. The protocol accumulates statistics fast enough to deliver single-molecule results from single-molecule experiments. We demonstrate the method’s performance by measuring the force-dependent kinetics of individual human β-cardiac myosin molecules interacting with an actin filament at physiological ATP concentration. We show that a molecule’s ADP release rate depends exponentially on the applied load, in qualitative agreement with cardiac muscle, which contracts with a velocity inversely proportional to external load.

https://www.ncbi.nlm.nih.gov/pubmed/26239258