Versatile Vibrational Energy Sensors for Proteins.

Autor: Löffler JG; Institute of Biophysics, Goethe University Frankfurt, Max-von-Laue-Straße 1, 60438, Frankfurt (Main), Germany., Deniz E; Institute of Biophysics, Goethe University Frankfurt, Max-von-Laue-Straße 1, 60438, Frankfurt (Main), Germany., Feid C; Institute of Biophysics, Goethe University Frankfurt, Max-von-Laue-Straße 1, 60438, Frankfurt (Main), Germany., Franz VG; Institute of Biophysics, Goethe University Frankfurt, Max-von-Laue-Straße 1, 60438, Frankfurt (Main), Germany., Bredenbeck J; Institute of Biophysics, Goethe University Frankfurt, Max-von-Laue-Straße 1, 60438, Frankfurt (Main), Germany.
Jazyk: angličtina
Zdroj: Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2022 May 16; Vol. 61 (21), pp. e202200648. Date of Electronic Publication: 2022 Apr 06.
DOI: 10.1002/anie.202200648
Abstrakt: Vibrational energy transfer (VET) is emerging as key mechanism for protein functions, possibly playing an important role for energy dissipation, allosteric regulation, and enzyme catalysis. A deep understanding of VET is required to elucidate its role in such processes. Ultrafast VIS-pump/IR-probe spectroscopy can detect pathways of VET in proteins. However, the requirement of having a VET donor and a VET sensor installed simultaneously limits the possible target proteins and sites; to increase their number we compare six IR labels regarding their utility as VET sensors. We compare these labels in terms of their FTIR, and VET signature in VET donor-sensor dipeptides in different solvents. Furthermore, we incorporated four of these labels in PDZ3 to assess their capabilities in more complex systems. Our results show that different IR labels can be used interchangeably, allowing for free choice of the right label depending on the system under investigation and the methods available.
(© 2022 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.)
Databáze: MEDLINE
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