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Additional file 4: Table S2. of The PINK1 p.I368N mutation affects protein stability and ubiquitin kinase activity

Year: 2017

Type: article

Abstract: FoldX measurement for mutational energy effect on stability of binding pocket. Using the FoldX algorithm, which compares the WT structure with the mutant, calculations on WT and mutant at t = 0 and after 100 ns were performed. While WT is nearly zero over that time interval, the N368 mutant increases energy (∆∆G) by 1.5–2 kcal/mol*Å2. This modest increase supports that the mutation distorts the local region via an increase of Gibb’s free energy. (DOCX 16 kb)

Source: Figshare

DOI: 10.6084/m9.figshare.4906076

Authors: Ando, Maya, Fiesel, Fabienne, Hudec, Roman, Caulfield, Thomas, Ogaki, Kotaro, Górka-Skoczylas, Paulina, Koziorowski, Dariusz, Friedman, Andrzej, Chen, Li, Dawson, Valina, Dawson, Ted, Bu, Guojun, Ross, Owen, Wszolek, Zbigniew, Springer, Wolfdieter

Language: English

Topic: Parkinson's Disease Mechanisms and Treatments

Subfield: Neurology

Field: Medicine

Domain: Health Sciences

Open Access status: green

OpenAlex ID: W7136043704

FWCI:

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