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Article

Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution.

Journal of the American Chemical Society - 10 Nov 2010

Dhulesia Anne, Cremades Nunilo, Kumita Janet R, Hsu Shang-Te Danny, Mossuto Maria F, Dumoulin Mireille, Nietlispach Daniel, Akke Mikael, Salvatella Xavier, Dobson Christopher M

Abstract excerpt

The partial unfolding of human lysozyme underlies its conversion from the soluble state into amyloid fibrils observed in a fatal hereditary form of systemic amyloidosis. To understand the molecular origins of the disease, it is critical to characterize the structural and physicochemical properties of the amyloidogenic states of the protein. Here we provide a high-resolution view of the unfolding process at low pH...

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Identifiers

PMID: 20958028
DOI: 10.1021/ja103524m
PMCID: PMC2974344

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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