Molecular Dynamics and Optimization Studies of α-Synuclein Protein Structures

Name: Molecular Dynamics and Optimization Studies of α-Synuclein Protein Structures
Brand: Springer Nature Switzerland AG
Price: 3270 SEK
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Mechanism Underlying the Parkinson’s Disease and Movement Disorders

AvJiapu Zhang

Springer Nature Switzerland AG

2026

Del i serien Springer Series in Biophysics

3 270 kr

Kommande

Beskrivning

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.

Produktinformation

Märke:Springer Nature Switzerland AG
Utgivningsdatum:2026-07-29
Höjd:155 x 235 x undefined mm
Språk:Engelska
Serie:Springer Series in Biophysics
Antal sidor:1 861
Förlag:Springer Nature Switzerland AG
EAN:9783032212801

Utforska kategorier

Biovetenskap inom Naturvetenskap och teknik
Biologi inom Naturvetenskap och teknik

Mer om författaren

Dr Jiapu Zhang received bachelor degree in 1993, first master degree in research in 1996, both from Qufu Normal University, P.R. China; second master degree in research in 2000 from National University of Singapore, Republic of Singapore; a PhD degree in 2005 from Federation University, Australia; and then a formal postdoctoral fellowship training from CSIRO (Commonwealth Scientific and Industrial Research Organisation), Australia. Dr Zhang also received honours in Australia and worldwide for his prion research. In 2011, the report of MIT (Massachusetts Institute of Technology) Technology Review on his prion results caused worldwide impacts so that several organizations (e.g., the Physics Society of Iran) published his prion results in seven languages. NHMRC (National Health and Medical Research Council) of Australia has assigned him review tasks on prion projects. CSIRO once conferred him an award (together with Drs Varghese JN and Epa VC) for rabbit prion protein research. He has been a reviewer for many top academic journals (e.g., Nature). All these made Dr Zhang feel honoured for his prion research. Dr Zhang also published one monograph by Springer in 2023 and 2024 for his SAR-COV-2 research "Optimization-based Molecular Dynamics Studies of SARS-CoV-2 Molecular Structures: Research on COVID- 19", in addition to two monographs on his prion research: "Molecular Dynamics Analyses of Prion Protein Structures: The Resistance to Prion Diseases Down Under", and "Molecular Structures and Structural Dynamics of Prion Proteins and Prions: Mechanism Underlying the Resistance to Prion Diseases", by the same Publisher.

Innehållsförteckning

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).