✍ Scribed by Hisakazu Mihara; Yuta Takahashi; Akihiko Ueno
No coin nor oath required. For personal study only.
Improved understanding of amyloidogenic peptides and proteins such as prion proteins and Alzheimer's b peptides has attracted much attention to the elucidation of the molecular mechanisms of such amyloidogenesis. As a representative, in the prion protein, the conformational transitions from a-helix to b-structure undergo along with the amyloidogenesis in a self-catalytic manner. Moreover, recent studies by the de novo design of peptides and proteins as well as the amyloidogenesis of peptides and proteins including pathogenic protein mutants have provided insight into the conformational changes essential to amyloidogenesis and correct folding.
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An improved understanding of protein misfolding is critical to the study of proteins involved in diseases such as Alzheimers and prion-related diseases, as well as to the clarification of the folding pathway of proteins. In general, hydrophobic clustering seems to be an important feature for peptide
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