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@proceedings{1874117, author = {Náplavová, Alexandra and Kozeleková, Aneta and Hritz, Jozef}, booktitle = {XXII. Workshop of Biophysical Chemists and Electrochemists.}, keywords = {14-3-3 protein, monomerization; dissociation constant; 19F NMR}, language = {eng}, isbn = {978-80-280-0087-5}, title = {Describing 14-3-3 dimerization: tools to obtain KD}, url = {https://www.sci.muni.cz/labifel/files/soubory/sbornik_2022.pdf}, year = {2022} }
TY - CONF ID - 1874117 AU - Náplavová, Alexandra - Kozeleková, Aneta - Hritz, Jozef PY - 2022 TI - Describing 14-3-3 dimerization: tools to obtain KD SN - 9788028000875 KW - 14-3-3 protein, monomerization KW - dissociation constant KW - 19F NMR UR - https://www.sci.muni.cz/labifel/files/soubory/sbornik_2022.pdf N2 - The self-association of proteins is one of the cornerstones of cellular processes. The oligomerization is a fundamental way of protein regulation, influencing their functionality and interactome [1]. Therefore, a strong need for quantitative analysis of oligomerization extent arises when studying proteins. A parameter especially useful for description of self-association is dissociation constant KD [2]. Such constant provides us picture of equilibrium between monomers and higher oligomers, at any given concentration. During our research, we focus closely on 14-3-3 proteins. 14-3-3s are regulators ubiquitous in eukaryotic cells, connected to neurodegenerative and oncologic diseases [3]. In their native state, dimers are formed, crucial for proper function [4]. However, it was revealed that phosphorylation at Ser58 of 14-3-3ζ leads to monomerization [5,6]. Here, we present an array of biophysical techniques used for oligomeric state quantification of several 14-3-3ζ constructs: wild type, phosphorylated at Ser58, monomeric and phosphomimicking mutants [5,7]. Contrary to majority of 14-3-3 studies, dimerization description via KD is not biased by used protein concentration. The importance of knowledge of KD is demonstrated, as differences in order of magnitude were discovered [5]. Moreover, workflow for KD determination via 19F Trp NMR is presented, exploiting that tryptophan is not only one of the rarest amino acids, but also has a unique role in protein self-association [8]. ER -
NÁPLAVOVÁ, Alexandra, Aneta KOZELEKOVÁ a Jozef HRITZ. Describing 14-3-3 dimerization: tools to obtain KD. In \textit{XXII. Workshop of Biophysical Chemists and Electrochemists.}. 2022. ISBN~978-80-280-0087-5.
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