Ultra-fast force-clamp spectroscopy data on the interaction between skeletal muscle myosin and actin.
Force-clamp spectroscopy
Myosin
Optical tweezers
Single molecule biophysics
Journal
Data in brief
ISSN: 2352-3409
Titre abrégé: Data Brief
Pays: Netherlands
ID NLM: 101654995
Informations de publication
Date de publication:
Aug 2019
Aug 2019
Historique:
received:
19
03
2019
revised:
30
04
2019
accepted:
10
05
2019
entrez:
22
6
2019
pubmed:
22
6
2019
medline:
22
6
2019
Statut:
epublish
Résumé
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].
Identifiants
pubmed: 31223637
doi: 10.1016/j.dib.2019.104017
pii: S2352-3409(19)30370-1
pii: 104017
pmc: PMC6565606
doi:
Types de publication
Journal Article
Langues
eng
Pagination
104017Références
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