@article {Sanjeev:2018:2212-7968:191,
title = "Dimerization of C-terminal Truncations of -synuclein and its Effect on the Aggregation Propensity: A Potential of Mean Force Study",
journal = "Current Chemical Biology",
parent_itemid = "infobike://ben/ccb",
publishercode ="ben",
year = "2018",
volume = "12",
number = "2",
publication date ="2018-08-01T00:00:00",
pages = "191-200",
itemtype = "ARTICLE",
issn = "2212-7968",
url = "https://www.ingentaconnect.com/content/ben/ccb/2018/00000012/00000002/art00011",
doi = "doi:10.2174/2212796812666180430143502",
keyword = "potential of mean force, truncation, molecular dynamics, Disordered, parkinson's disease, α-
synuclein",
author = "Sanjeev, Airy and Mattaparthi, Venkata S. K.",
abstract = "Background: The occurrence of Parkinson's Disease (PD) is associated with the deposition of proteinaceous aggregates formed by the self-assembly of -synuclein protein. The pathogenesis of PD has been reported to be linked with the -synuclein gene. However, the presence
of missense mutations: A30P, A53T, E46K, H50Q, G51D and A53E has also been linked with the autosomal inheritance of PD. Recently, it has been highlighted that C-terminal truncated -synucleins undergo aggregation at a faster rate while the full-length -synucleins are critical.
Objective: To study the dimerization of C-terminal truncations of -synuclein and its effect on the aggregation propensity. Methodology: We investigated the dimerization of the two important C-terminal truncations (120 and 123) of -synuclein using Molecular Dynamics
Simulation and Potential of Mean Force (PMF) study. Results: From our PMF study, we observed that the binding free energy value to be larger for the association of C-terminal truncated -synucleins than the value that has been reported for Wild-Type (WT) in our earlier study. 
Conclusion: Truncating the C-terminal region (which is considered to be intra-molecular chaperone) in -synucleins exposes the hydrophobic region and thereby increases the aggregation propensity.",
}