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Article

Disulfide engineering reveals unexpected pro- and anti-aggregation conformers of human α-synuclein

2026-01-08

Abstract excerpt

Intrinsically disordered proteins can aggregate in many distinct conformations (polymorphs). Polymorphs are a striking example of fold-switching: one primary structure able to form distinct tertiary structures. Distinct polymorphs can yield distinct molecular, cellular, and disease phenotypes. Disulfide crosslinks canalize disordered proteins into distinct regions of the conformational landscape, even if the monom...

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Literature Corpus work
892be75b-0c91-5e42-a20f-6822c3156702
DOI
10.64898/2026.01.07.698305
Open publication

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Disulfide engineering reveals unexpected pro- and anti-aggregation conformers of human α-synucleinDOI 10.64898/2026.01.07.698305
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