Impact of Phosphorylation for Tau210-240 Peptide and Interaction of Small Molecules and 14-3-3ζ Protein Studies Using Computational Methods
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| Year of publication | 2022 |
| Type | Appeared in Conference without Proceedings |
| MU Faculty or unit | |
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| Description | The conformational dynamics of intrinsically disordered proteins (IDPs) regulated by post-translational modifications such as phosphorylation is challenging to elucidate. A well-known IDP Tau is found hyper-phosphorylated in Alzheimer’s disease (AD) in humans [1]. The proline-rich motif of Tau210-240 peptide directly interacts with proteins such as 14-3-3?. 14-3-3? is one of the crucial protein in the human brain and bind to a multiarray of proteins. It has a significant impact on forming and deforming neurofibrillary tangles, and it was shown that the 14-3-3? monomer has strong anti-aggregation properties [2]. It was shown that monomerization of 14-3-3z can be induced by phosphorylation of Ser58 at the dimeric interface |
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