关于骨骼肌肌球蛋白与肌动蛋白相互作用的超快力钳光谱数据。

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

作者信息

Maffei Manuela, Beneventi Diego, Canepari Monica, Bottinelli Roberto, Pavone Francesco Saverio, Capitanio Marco

机构信息

Department of Molecular Medicine, University of Pavia, Pavia, Italy.

LENS - European Laboratory for Non-linear Spectroscopy, Via Nello Carrara 1, 50019 Sesto Fiorentino, Italy.

出版信息

Data Brief. 2019 May 23;25:104017. doi: 10.1016/j.dib.2019.104017. eCollection 2019 Aug.

DOI:10.1016/j.dib.2019.104017

PMID:31223637

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6565606/

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].

摘要

超快力钳光谱技术是一种基于激光镊子的单分子技术，具有亚毫秒和亚纳米分辨率。该技术已成功应用于研究骨骼肌中的肌球蛋白II马达与肌动蛋白丝相互作用时发生的快速构象变化。在这里，我们分享了这种相互作用的动力学数据以及在不同力作用下收集的实验记录[1]。从实验和建模的角度来看，这些数据对于对肌球蛋白II的机械敏感特性感兴趣的研究人员可能很有价值。这些数据与研究文章《单分子超快力钳光谱揭示肌球蛋白工作行程的负载依赖性》[2]相关。