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Structural Analysis of SOD1 Fibrils with Mass Spectrometry, Limited Proteolysis, and Atomic Force Microscopy (AFM).

Methods in molecular biology (Clifton, N.J.) - 1 Jan 2023

Koo Bon-Kyung, Whitelegge Julian

Abstract excerpt

This protocol describes a method to purify SOD1 in Saccharomyces cerevisiae to characterize using ICP-MS and AFM, to agitate and fibrillate for aggregation of SOD1. The human SOD1 (hSOD1) is a 32-kDa homodimer, with one copper- and one zinc-binding site per 153-amino acid subunit. Misfolded protein aggregates are often correlated with diseases known as amyloidosis, including ALS, Alzheimer's, Parkinson's, and...

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PMID: 36310221
DOI: 10.1007/978-1-0716-2597-2_30

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