Computational approach to study protein structural properties and transformations
2017
Southern Medical University, Guangzhou, China
Alpha-synuclein is a protein with a significant role in several diseases known as synucleinopathies. Its dimerization can trigger conformational transformations critical for its aggregation and the formation of fibrils. In this study, molecular dynamics simulations are used to investigate the mechanisms of dimerization of alpha-synuclein and its structural properties. The results show that, effectively, the monomers undergo a series of conformational transformations and they can resolve several structural features that are consistent with current experimental observations. These transformations lead to intermolecular interactions that contribute to the formation and stabilization of alpha-synuclein dimers. The researchers present a computational strategy that can help to design small molecules that can inhibit the pathological processes that lead to alpha-synuclein aggregation.
Molecular dynamics study to investigate the dimeric structure of the full-length α-synuclein in aqueous solution
Shuwen Liu, Jiajie Zhang
Added on: 08-10-2021
[1] https://pubs.acs.org/doi/10.1021/acs.jcim.7b00210[2] https://data.jrc.ec.europa.eu/dataset/a8fd26ef-b113-47ab-92ba-fd2be449c7eb
