Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 79, Issue 3, Pages 937-946Publisher
WILEY
DOI: 10.1002/prot.22935
Keywords
protein structure; molecular mechanics; amyloid; polyglutamine; protein aggregation
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Funding
- NSF [FRG-0804549]
- Division Of Materials Research
- Direct For Mathematical & Physical Scien [804549] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1021883] Funding Source: National Science Foundation
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The alpha-sheet has been speculated to play a role as a toxic conformer in amyloid diseases. However, except for relatively short fragments, its detection has remained elusive. Here, we present molecular dynamics simulations that support the existence of the alpha-sheet as a stable, metastable, or long-lived secondary structure in polyglutamine and, to a lesser extent, in polyasparagine aggregates.
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