Molecular Dynamics and Optimization Studies of -Synuclein Protein Structures, m. 2 Buch : Mechanism Underlying the Parkinson's Disease and Movement Disorders (Springer Series in Biophysics)

Zhang, Jiapu

Springer, Berlin; Springer（2026/07発売）

• 商品コード 9783032212801

Full Description

Parkinson's disease (PD), the second most common neurodegenerative disorder in human. The cause of PD is believed to involve genetic factors. At least 6 pathogenic genes have been associated with familial PD. α-Synuclein (αS) is the main component of the Lewy bodies that accumulate in the brains of people with PD. Misfolding of the αS protein has been implicated in the molecular chain of events leading to PD. This book studies wild type (WT) αS proteins and their (8) αS(1-140)-mutants by optimization and Molecular Dynamics (MD). In this book our systematic MD study of a wider range of mutants would provide some answers for genetic factors.

Numerous bindings of some segments of αS are also MD studied. Some fibrils leaded by aS misfolding are MD studied too.

This book is particularly valuable for professionals working in computing roles within computational biochemistry/biophysics, bioinformatics, etc. It serves as an accessible introduction and is an excellent resource for students.

Contents

Structures and functions of the a-Synuclein (aS) protein.- aS WTs.- aS A30P-variant.- aS E35K-variant.- aS E46K variant.- aS H50Q variant.- aS G51D variant.- aS A53T variant.- aS A53T-V40D-V74D variant.- aS E57K variant.- aS(1-12) binging with Synphilin-1(510-557).- aS(1-19) binding with calmodulin(1-148).- aS(135-140) binding with camelid antibody NbSyn2(2-127).- aS(121-140) binding with fifty ligands.- aS(35-56) binding with bW(13-58).- aS(31-41) binding with PDI(208-449).- aS(29-49) binding with 50 ligands.- aS(1-140) binding with four ligands.- Seven XKTKEGVXXXX repeats in aS(1-91).