期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 136, 期 43, 页码 15146-15149出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja508621b
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资金
- NSF
- NASA Astrobiology Program [CHE-1004560]
- U.S. Department of Energy [DE-ER15377]
In contrast to an expected Ostwald-like ripening of amyloid assemblies, the nucleating core of the Dutch mutant of the A beta peptide of Alzheimers disease assembles through a series of conformational transitions. Structural characterization of the intermediate assemblies by isotope-edited IR and solid-state NMR reveals unexpected strand orientation intermediates and suggests new nucleation mechanisms in a progressive assembly pathway.
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