Mutations in position 129 of the human prion protien 1 Multiple substitutions of Methionine 129 in Human Prion Protein Reveal its Importance in the Amyloid Fibrillation Pathway
نویسندگان
چکیده
Background: A polymorphism in position 129 in the human prion protein modulates susceptibility to prion infection and disease phenotype. Results: Mutations to various amino acids highlights the importance of position 129 during amyloid fibrillation. Conclusion: Position 129 is a key site for early intermolecular interactions during fibrillation. Significance: Insight into early mechanisms of aggregation implicates a means to prevent fibrillation
منابع مشابه
Multiple substitutions of methionine 129 in human prion protein reveal its importance in the amyloid fibrillation pathway.
The role of the polymorphism Met or Val in position 129 in the human prion protein is well documented regarding disease susceptibility and clinical manifestations. However, little is known about the molecular background to this phenomenon. We investigated herein the conformational stability, amyloid fibrillation kinetics, and seeding propensity of different 129 mutants, located in β-strand 1 of...
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