scholarly journals Investigation on the conformational conversion of human prion protein by molecular dynamics simulation

2017 ◽  
Author(s):  
◽  
Hong Yang
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Prion Protein ◽  
Dynamics Simulation ◽  
Human Prion Protein ◽  
Conformational Conversion

scholarly journals Molecular Dynamics Simulation of Dimeric and Monomeric Forms of Human Prion Protein: Insight into Dynamics and Properties

2003 ◽  
Vol 85 (2) ◽  
pp. 1176-1185 ◽  
Author(s):  
Masakazu Sekijima ◽  
Chie Motono ◽  
Satoshi Yamasaki ◽  
Kiyotoshi Kaneko ◽  
Yutaka Akiyama
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Prion Protein ◽  
Dynamics Simulation ◽  
Human Prion Protein ◽  
Insight Into

scholarly journals Human Prion Protein Conformational Changes Susceptibility: A Molecular Dynamics Simulation Study

2014 ◽  
Vol 04 (04) ◽  
pp. 169-175 ◽  
Author(s):  
Laura Alejandra Mandujano-Rosas ◽  
Daniel Osorio-González ◽  
Pedro Guillermo Reyes-Romero ◽  
Jorge Mulia-Rodríguez
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Prion Protein ◽  
Conformational Changes ◽  
Simulation Study ◽  
Dynamics Simulation ◽  
Protein Conformational Changes ◽  
Human Prion Protein

scholarly journals 2P049 Molecular dynamics simulation on Prion Protein: effect of P102L mutation

2004 ◽  
Vol 44 (supplement) ◽  
pp. S122
Author(s):  
M. Sekijima ◽  
C. Motono ◽  
T. Noguchi ◽  
K. Kaneko ◽  
Y. Akiyama
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Prion Protein ◽  
Dynamics Simulation

scholarly journals Molecular dynamics simulation reveals that switchable combinations of β-sheets underlie the prion-like properties of α-synuclein amyloids

2018 ◽  
Author(s):  
Hiroki Otaki ◽  
Yuzuru Taguchi ◽  
Noriyuki Nishida
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Prion Protein ◽  
Dynamics Simulation ◽  
Protein Species ◽  
Strain Diversity ◽  
Prion Strains ◽  
Parkinson’S Diseases ◽  
Single Protein ◽  
Β Sheets

AbstractDiversity of prion strains is one of the most mysterious traits of prions because they are mere aggregates of abnormally-folded forms of single protein species, prion protein (PrPSc), without genome. Although the strain-specific properties are hypothesized to be enciphered in the strain-specific structures of PrPSc instead of nucleotide genome, specifically what structure can code the information remains an enigma due to the incompatibility of PrPSc with structural analyses. Although the strain diversity was regarded as unique to prions, recently other disease-associated amyloids of α-synuclein (αSyn) or tau are also reported to have “strains”. As detailed structures of αSyn amyloid are already identified and the properties of mutant αSyn associated with familial Parkinson’s diseases, e.g. A53T, H50Q, and G51D, have been characterized, structure-phenotype relations of this type of amyloid could be investigated by using the αSyn amyloid as a model. Here we intensively investigated the mutant αSyn amyloids by molecular dynamics simulation to characterize influences of mutations on the structures of homo- or hetero-oligomer stacks of the amyloid. The simulations revealed directionality of the amyloid stack, remote effects of the mutations on distant β-sheets, existence of at least two switchable interfaces/amyloid cores, and distinct effects of hetero-oligomerization depending on mutation types. Collectively, those findings implied a possible mechanism of the strain diversity of the amyloids which have multiple in-register parallel β-sheets side-by-side, and support the view that their prion-like properties are inherent in the characteristic structures. We expect that the notion is also applicable to PrPSc.

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