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Using azobenzene photocontrol to set proteins in motion


Bozovic, Olga; Jankovic, Brankica; Hamm, Peter (2022). Using azobenzene photocontrol to set proteins in motion. Nature Reviews Chemistry, 6(2):112-124.

Abstract

Controlling the activity of proteins with azobenzene photoswitches is a potent tool for manipulating their biological function. With the help of light, it is possible to change binding affinities, control allostery or manipulate complex biological processes, for example. Additionally, owing to their intrinsically fast photoisomerization, azobenzene photoswitches can serve as triggers that initiate out-of-equilibrium processes. Such switching of the activity initiates a cascade of conformational events that can be accessed with time-resolved methods. In this Review, we show how the potency of azobenzene photoswitching can be combined with transient spectroscopic techniques to disclose the order of events and experimentally observe biomolecular interactions in real time. This strategy will further our understanding of how a protein can accommodate, adapt and readjust its structure to answer an incoming signal, revealing more of the dynamical character of proteins.

Abstract

Controlling the activity of proteins with azobenzene photoswitches is a potent tool for manipulating their biological function. With the help of light, it is possible to change binding affinities, control allostery or manipulate complex biological processes, for example. Additionally, owing to their intrinsically fast photoisomerization, azobenzene photoswitches can serve as triggers that initiate out-of-equilibrium processes. Such switching of the activity initiates a cascade of conformational events that can be accessed with time-resolved methods. In this Review, we show how the potency of azobenzene photoswitching can be combined with transient spectroscopic techniques to disclose the order of events and experimentally observe biomolecular interactions in real time. This strategy will further our understanding of how a protein can accommodate, adapt and readjust its structure to answer an incoming signal, revealing more of the dynamical character of proteins.

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Additional indexing

Item Type:Journal Article, refereed, further contribution
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Uncontrolled Keywords:General Chemical Engineering, General Chemistry
Language:English
Date:1 February 2022
Deposited On:09 Dec 2021 04:25
Last Modified:26 Apr 2024 01:37
Publisher:Springer
ISSN:2397-3358
OA Status:Green
Publisher DOI:https://doi.org/10.1038/s41570-021-00338-6
Project Information:
  • : FunderSNSF
  • : Grant ID200021_165789
  • : Project TitleUltrafast Vibrational Spectroscopy of Allosteric Proteins
  • : FunderSNSF
  • : Grant ID200020B_188694
  • : Project TitleUltrafast Vibrational Spectroscopy of Allosteric Proteins (Extension)
  • : FunderFP7
  • : Grant ID246646
  • : Project TitleTowards a Dynamical Understanding of Allostery