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- W2063364823 abstract "Information is provided about the amino acid residues in the [1–28] domain of the Alzheimer β-amyloid protein, which participate in interstrand pairing and initiate fibillogenesis. The study was carried out using electrospray ionization on a four sector mass spectrometer, measuring kinetic energy release for a fragmentation process, and modeling the transition state with molecular dynamics calculations. The results eliminate the sequence [11–24] proposed earlier as the central core, and are consistent with, but do not distinguish between, residues [17–28] and [17–23] proposed by others based on biochemical studies." @default.
- W2063364823 created "2016-06-24" @default.
- W2063364823 creator A5031750652 @default.
- W2063364823 creator A5072485510 @default.
- W2063364823 date "2004-04-01" @default.
- W2063364823 modified "2023-10-14" @default.
- W2063364823 title "Contact Regions in the Dimer of Alzheimer β-Amyloid Domain [1–28] Studied by Mass Spectrometry" @default.
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- W2063364823 doi "https://doi.org/10.1255/ejms.642" @default.
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