Title : Extremely Amyloidogenic Single-Chain Analogues of Insulin's H-Fragment: Structural Adaptability of an Amyloid Stretch.

Pub. Date : 2020 Oct 20

PMID : 32988199






3 Functional Relationships(s)
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1 Here, we focus on the highly amyloidogenic H-fragment of insulin comprising the disulfide-bonded N-terminal parts of both chains. Disulfides insulin Homo sapiens
2 Our study suggests that the N-terminal part of insulin"s A-chain containing the intact Cys6-Cys11 intrachain disulfide bond may constitute insulin"s major amyloid stretch which, through its bent conformation, enforces a parallel in-register alignment of beta-strands. Disulfides insulin Homo sapiens
3 Our study suggests that the N-terminal part of insulin"s A-chain containing the intact Cys6-Cys11 intrachain disulfide bond may constitute insulin"s major amyloid stretch which, through its bent conformation, enforces a parallel in-register alignment of beta-strands. Disulfides insulin Homo sapiens