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Article

Exploring the aggregation free energy landscape of the amyloid-β protein (1-40).

Proceedings of the National Academy of Sciences of the United States of America - 18 Oct 2016

Zheng Weihua, Tsai Min-Yeh, Chen Mingchen, Wolynes Peter G

Abstract excerpt

A predictive coarse-grained protein force field [associative memory, water-mediated, structure, and energy model for molecular dynamics (AWSEM)-MD] is used to study the energy landscapes and relative stabilities of amyloid-β protein (1-40) in the monomer and all of its oligomeric forms up to an octamer. We find that an isolated monomer is mainly disordered with a short α-helix formed at the central hydrophobic...

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Identifiers

PMID: 27698130
DOI: 10.1073/pnas.1612362113
PMCID: PMC5081630

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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