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- W2024657188 abstract "Copper, zinc superoxide dismutase 1 (SOD1) is a ubiquitous homodimeric enzyme, whose misfolding and aggregation play a potentially key role in the neurodegenerative disease amyotrophic lateral sclerosis (ALS). SOD1 aggregation is thought to be preceded by dimer dissociation and metal loss, but the mechanisms by which the metal-free monomer aggregates remain incompletely understood. Here we use implicit solvent all-atom Monte Carlo (MC) methods to investigate the local unfolding dynamics of the β-barrel-forming SOD1 monomer. Although event-to-event variations are large, on average, we find clear differences in dynamics among the eight strands forming the β-barrel. Most dynamic is the eighth strand, β8, which is located in the dimer interface of native SOD1. For the four strands in or near the dimer interface (β1, β2, β7, and β8), we perform aggregation simulations to assess the propensity of these chain segments to self-associate. We find that β1 and β2 readily self-associate to form intermolecular parallel β-sheets, whereas β8 shows a very low aggregation propensity." @default.
- W2024657188 created "2016-06-24" @default.
- W2024657188 creator A5023319008 @default.
- W2024657188 creator A5060442147 @default.
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- W2024657188 date "2013-07-25" @default.
- W2024657188 modified "2023-09-27" @default.
- W2024657188 title "Local Unfolding and Aggregation Mechanisms of SOD1: A Monte Carlo Exploration" @default.
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- W2024657188 doi "https://doi.org/10.1021/jp404500b" @default.
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