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Triplet States Reveal Slow Local Dynamics in the Solvation Shell of Biomolecules.

Weigl, Peter ; Weißheit, Susann ; Pabst, Florian ; Kolmar, Harald ; Thiele, Christina Marie ; Walther, Thomas ; Blochowicz, Thomas (2022)
Triplet States Reveal Slow Local Dynamics in the Solvation Shell of Biomolecules.
In: The Journal of Physical Chemistry B, 126 (33)
doi: 10.1021/acs.jpcb.2c03784
Article, Bibliographie

Abstract

Protein hydration shell dynamics plays a pivotal role in biochemical processes such as protein folding, enzyme function, molecular recognition and interaction with biological membranes. Thus, it is crucial to understand the mobility of the solvation shell at the surface of biomolecules. Triplet state solvation dynamics can reveal the slow dynamics of the solvation shell. This is done in the present work without adding separate dye molecules but instead by using a phosphorescent subgroup of the biomolecule itself. In particular, we study a small heptapeptide in a glycerol-water mixture under cryoconservation conditions so that the system can be supercooled without crystallization. We find a significant slowing of molecules in the solvation shell in the millisecond range compared to the bulk. This opens up the possibility to unravel the nature of relaxation processes in the solvation shell usually overlapping at room temperature.

Item Type: Article
Erschienen: 2022
Creators: Weigl, Peter ; Weißheit, Susann ; Pabst, Florian ; Kolmar, Harald ; Thiele, Christina Marie ; Walther, Thomas ; Blochowicz, Thomas
Type of entry: Bibliographie
Title: Triplet States Reveal Slow Local Dynamics in the Solvation Shell of Biomolecules.
Language: English
Date: 25 August 2022
Publisher: ACS Publications
Journal or Publication Title: The Journal of Physical Chemistry B
Volume of the journal: 126
Issue Number: 33
DOI: 10.1021/acs.jpcb.2c03784
Abstract:

Protein hydration shell dynamics plays a pivotal role in biochemical processes such as protein folding, enzyme function, molecular recognition and interaction with biological membranes. Thus, it is crucial to understand the mobility of the solvation shell at the surface of biomolecules. Triplet state solvation dynamics can reveal the slow dynamics of the solvation shell. This is done in the present work without adding separate dye molecules but instead by using a phosphorescent subgroup of the biomolecule itself. In particular, we study a small heptapeptide in a glycerol-water mixture under cryoconservation conditions so that the system can be supercooled without crystallization. We find a significant slowing of molecules in the solvation shell in the millisecond range compared to the bulk. This opens up the possibility to unravel the nature of relaxation processes in the solvation shell usually overlapping at room temperature.

Identification Number: pmid:35973008
Divisions: 05 Department of Physics
05 Department of Physics > Institute for Condensed Matter Physics
05 Department of Physics > Institute for Condensed Matter Physics > Struktur und Dynamik amorpher Systeme
Date Deposited: 30 Aug 2022 08:37
Last Modified: 30 Aug 2022 08:37
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