Journal Article

FZJ-2023-02080

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Complementary approaches to obtaining thermodynamic parameters from protein ligand systems-challenges and opportunities

Sarter, M. (Corresponding author) ; Niether, D. ; Wiegand, S.FZJ* ; Fitter, J.FZJ* ; Stadler, A. M.FZJ*

2022
EDP Sciences Les Ulis

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Please use a persistent id in citations: http://hdl.handle.net/2128/34450  doi:10.1051/epjconf/202227201016

Abstract: Protein ligand interactions play an important role in biology. Increasingly the aim is to understandand influence protein ligand binding. The binding process is heavily influenced by its thermodynamicparameters. In order to understand how the whole system thermodynamics work it is important to characterisethe individual contribution of each of the systems components. While the change in conformational entropyof the protein can be determined using QENS complementary methods are necessary in order to characteriseall components. This paper will describe the challenges that can occur when combining the different methods,as well as how they can be overcome.

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Contributing Institute(s):

1. Zelluläre Strukturbiologie (IBI-6)
2. Strukturbiologie (ER-C-3)
3. Neutronenstreuung (JCNS-1)
4. Neutronenstreuung und biologische Materie (IBI-8)
5. Biomakromolekulare Systeme und Prozesse (IBI-4)

Research Program(s):

1. 5352 - Understanding the Functionality of Soft Matter and Biomolecular Systems (POF4-535) (POF4-535)
2. 5241 - Molecular Information Processing in Cellular Systems (POF4-524) (POF4-524)

Appears in the scientific report 2023

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Database coverage:
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