Conformational dynamics of a single protein monitored for 24 hours at video rate
Abstract
We use plasmon rulers to follow the conformational dynamics of a single protein for up to 24 h at a video rate. The plasmon ruler consists of two gold nanospheres connected by a single protein linker. In our experiment, we follow the dynamics of the molecular chaperone heat shock protein 90, which is known to show open and closed conformations. Our measurements confirm the previously known conformational dynamics with transition times in the second to minute time scale and reveals new dynamics on the time scale of minutes to hours. Plasmon rulers thus extend the observation bandwidth 3/4 orders of magnitude with respect to single-molecule fluorescence resonance energy transfer and enable the study of molecular dynamics with unprecedented precision.
Keywords
Cite
@article{arxiv.1806.07156,
title = {Conformational dynamics of a single protein monitored for 24 hours at video rate},
author = {Weixiang Ye and Markus Götz and Sirin Celiksoy and Laura Tüting and Christoph Ratzke and Janak Prasad and Rubén Ahijado-Guzmán and Thorsten Hugel and Carsten Sönnichsen},
journal= {arXiv preprint arXiv:1806.07156},
year = {2018}
}