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TitleElectrostatics of tau protein by molecular dynamics
Author(s)Castro, Tarsila Gabriel
Munteanu, Florentina-Daniela
Cavaco-Paulo, Artur
Protein structure prediction
Molecular modelling
Molecular dynamics
Taumicrotubule association
Issue dateMar-2019
PublisherMultidisciplinary Digital Publishing Institute (MDPI)
CitationCastro, T.; Munteanu, Florentina-Daniela; Cavaco-Paulo, Artur, Electrostatics of tau protein by molecular dynamics. Biomolecules, 9(3), 116, 2019
Abstract(s)Tau is a microtubule-associated protein that promotes microtubule assembly and stability. This protein is implicated in several neurodegenerative diseases, including Alzheimer’s. To date, the three-dimensional (3D) structure of tau has not been fully solved, experimentally. Even the most recent information is sometimes controversial in regard to how this protein folds, interacts, and behaves. Predicting the tau structure and its profile sheds light on the knowledge about its properties and biological function, such as the binding to microtubules (MT) and, for instance, the effect on ionic conductivity. Our findings on the tau structure suggest a disordered protein, with discrete portions of well-defined secondary structure, mostly at the microtubule binding region. In addition, the first molecular dynamics simulation of full-length tau along with an MT section was performed, unveiling tau structure when associated with MT and interaction sites. Electrostatics and conductivity were also examined to understand how tau affects the ions in the intracellular fluid environment. Our results bring a new insight into tau and tubulin MT proteins, their characteristics, and the structure–function relationship.
Publisher version
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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