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Ultra-fast Force-clamp Spectroscopy Data on the Interaction Between Skeletal Muscle Myosin and Actin

Overview
Journal Data Brief
Date 2019 Jun 22
PMID 31223637
Citations 3
Authors
Manuela Maffei
Diego Beneventi
Monica Canepari
Roberto Bottinelli
Francesco Saverio Pavone
Marco Capitanio
Affiliations
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Abstract

Ultrafast force-clamp spectroscopy is a single molecule technique based on laser tweezers with sub-millisecond and sub-nanometer resolution. The technique has been successfully applied to investigate the rapid conformational changes that occur when a myosin II motor from skeletal muscle interacts with an actin filament. Here, we share data on the kinetics of such interaction and experimental records collected under different forces [1]. The data can be valuable for researchers interested in the mechanosensitive properties of myosin II, both from an experimental and modeling point of view. The data is related to the research article "ultrafast force-clamp spectroscopy of single molecules reveals load dependence of myosin working stroke" [2].

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Out-of-Equilibrium Biophysical Chemistry: The Case for Multidimensional, Integrated Single-Molecule Approaches.

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Ultra-fast force-clamp spectroscopy data on the interaction between skeletal muscle myosin and actin.

Maffei M, Beneventi D, Canepari M, Bottinelli R, Pavone F, Capitanio M Data Brief. 2019; 25:104017.

PMID: 31223637 PMC: 6565606. DOI: 10.1016/j.dib.2019.104017.

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Maffei M, Beneventi D, Canepari M, Bottinelli R, Pavone F, Capitanio M . Ultra-fast force-clamp spectroscopy data on the interaction between skeletal muscle myosin and actin. Data Brief. 2019; 25:104017. PMC: 6565606. DOI: 10.1016/j.dib.2019.104017. View
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