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The Speed of Allosteric Signaling Within a Single-Domain Protein

Božović, Olga; Ruf, Jeannette; Zanobini, Claudio; Jankovic, Brankica; Buhrke, David; Johnson, Philip J M; Hamm, Peter (2021). The Speed of Allosteric Signaling Within a Single-Domain Protein. Journal of Physical Chemistry Letters, 12(17):4262-4267.

Abstract

While much is known about different allosteric regulation mechanisms, the nature of the allosteric signal and the time scale on which it propagates remains elusive. The PDZ3 domain from postsynaptic density-95 protein is a small protein domain with a terminal third α-helix, i.e., the α3-helix, which is known to be allosterically active. By cross-linking the allosteric helix with an azobenzene moiety, we obtained a photocontrollable PDZ3 variant. Photoswitching triggers its allosteric transition, resulting in a change in binding affinity of a peptide to the remote binding pocket. Using time-resolved infrared and UV/vis spectroscopy, we follow the allosteric signal transduction and reconstruct the timeline in which the allosteric signal propagates through the protein within 200 ns.

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Scopus Subject Areas:Physical Sciences > General Materials Science
Physical Sciences > Physical and Theoretical Chemistry
Uncontrolled Keywords:General Materials Science, Physical and Theoretical Chemistry
Language:English
Date:6 May 2021
Deposited On:20 Oct 2021 12:55
Last Modified:25 Jan 2025 02:42
Publisher:American Chemical Society (ACS)
ISSN:1948-7185
OA Status:Green
Publisher DOI:https://doi.org/10.1021/acs.jpclett.1c00915
PubMed ID:33904738
Project Information:
  • Funder: SNSF
  • Grant ID: 200020B_188694
  • Project Title: Ultrafast Vibrational Spectroscopy of Allosteric Proteins (Extension)
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