Conformational dynamics of a single protein monitored for 24 hours at video rate

TL;DR

This study demonstrates the use of plasmon rulers to monitor the conformational dynamics of a single protein, heat shock protein 90, over 24 hours at video rate, revealing both known and new dynamics.

Contribution

The paper introduces plasmon rulers as a tool for long-term, high-resolution observation of single-protein conformational changes, extending the observation window significantly.

Findings

Confirmed known conformational transition times of seconds to minutes.

Discovered new dynamics occurring over minutes to hours.

Extended observation bandwidth by 3/4 orders of magnitude compared to fluorescence methods.

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.