Design of peptides undergoing self-catalytic α-to-β transition and amyloidogenesis
作者： Hisakazu Mihara , Yuta Takahashi , Akihiko Ueno
DOI: 10.1002/(SICI)1097-0282(1998)47:1<83::AID-BIP9>3.0.CO;2-T
关键词: Mutant 、 Chemistry 、 Combinatorial chemistry 、 Biochemistry 、 Protein folding 、 Prion protein 、 Folding (chemistry) 、 Transition (genetics) 、 Prion Proteins 、 Biophysics 、 Organic chemistry 、 Biomaterials 、 General Medicine
摘要: Improved understanding of amyloidogenic peptides and proteins such as prion Alzheimer's beta has attracted much attention to the elucidation molecular mechanisms amyloidogenesis. As a representative, in protein, conformational transitions from alpha-helix beta-structure undergo along with amyloidogenesis self-catalytic manner. Moreover, recent studies by de novo design well including pathogenic protein mutants have provided insight into changes essential correct folding.
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