Using Azobenzene Photocontrol to Set Proteins in Motion

TL;DR

This paper reviews how azobenzene photoswitches, combined with transient spectroscopy, enable real-time observation of protein conformational changes and interactions, advancing understanding of protein dynamics and control.

Contribution

It introduces the integration of azobenzene photoswitches with time-resolved spectroscopic techniques to study protein conformational dynamics in real-time.

Findings

Azobenzene photoswitches can control protein activity with light.

Time-resolved spectroscopy reveals the sequence of conformational events.

This approach enhances understanding of protein structural adaptation.

Abstract

Controlling the activity of proteins with azobenzene photoswitches is a potent tool for manipulating their biological function. With the help of light, one can change e.g. binding affinities, control allostery or temper with complex biological processes. Additionally, due to their intrinsically fast photoisomerisation, azobenzene photoswitches can serve as triggers to initiate out-of-equilibrium processes. Such switching of the activity, therefore, initiates a cascade of conformational events, which can only be accessed with time-resolved methods. In this Review, we will show how combining the potency of azobenzene photoswitching with transient spectroscopic techniques helps to disclose the order of events and provide an experimental observation of biomolecular interactions in real-time. This will ultimately help us to understand how proteins accommodate, adapt and readjust their structure to answer an incoming signal and it will complete our knowledge of the dynamical character of proteins.