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@proceedings{1751020,
author = {Bera, Krishnendu and Lasorsa, A. and Malki, I. and Dupre, E. and Cantrelle, F.X. and Merzougui, H. and Sinnaeve, D. and Hanoulle, X. and Hritz, Jozef and Landrieu, I.},
keywords = {Molecular Dynamic Simulation; Tau210-240},
language = {eng},
title = {Study of Conformational and Dynamic Changes upon Phosphorylation of Proline Rich Region of Tau210-240 Peptide Using Molecular Dynamic Simulation},
url = {https://www.ceitec.eu/abstract-book-2021-final-pdf/f43850},
year = {2021}
}
TY - CONF
ID - 1751020
AU - Bera, Krishnendu - Lasorsa, A. - Malki, I. - Dupre, E. - Cantrelle, F.X. - Merzougui, H. - Sinnaeve, D. - Hanoulle, X. - Hritz, Jozef - Landrieu, I.
PY - 2021
TI - Study of Conformational and Dynamic Changes upon Phosphorylation of Proline Rich Region of Tau210-240 Peptide Using Molecular Dynamic Simulation
KW - Molecular Dynamic Simulation
KW - Tau210-240
UR - https://www.ceitec.eu/abstract-book-2021-final-pdf/f43850
N2 - The conformational and dynamic changes of protein interaction regulated by posttranslational modifications such as phosphorylation of intrinsically disordered proteins (IDPs), remains challenging to elucidate. Tau, which is a well-known IDP and its phosphorylation is of particular interest because Tau is found hyperthe conformational and dynamic changes upon phosphorylation of Tau. The proline-rich motif recognized within Tau210-240 peptide directly interact with AD progression protein such as 14-3-3. Microsecond time scale molecular dynamic simulation studies performed for apo and phosphorylated residues (212PThr, 217PThr, 231PThr, 235PSer) Tau peptide210-240 using three different temperature variants (278° K, 298° K and 310° K) and two different force field parameters (AMBER99SB-ILDN and CHARMM36m) with TIP4PD water model. These four-phosphorylation causing increase in compactness. The strong salt bridges are forming with nearby lysine and arginine due to the phosphorylation, which may alter the binding of associated protein like 14-3-3 with Tau. Phosphorylation induces a strong structural transition, with Tau210 240 favouring a bent conformation. The MD simulation results were verified using NMR experimental parameters like chemical shift, 3J-coupling etc. The experimental part has been carried out by our collaborator Prof. Isabelle Landrieu.
ER -
BERA, Krishnendu, A. LASORSA, I. MALKI, E. DUPRE, F.X. CANTRELLE, H. MERZOUGUI, D. SINNAEVE, X. HANOULLE, Jozef HRITZ a I. LANDRIEU. \textit{Study of Conformational and Dynamic Changes upon Phosphorylation of Proline Rich Region of Tau210-240 Peptide Using Molecular Dynamic Simulation}. 2021.
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