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Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance
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- Olofsson, Anders (author)
- Umeå universitet,Umeå centrum för molekylär patogenes (UCMP)
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- Sauer-Eriksson, A Elisabeth (author)
- Umeå universitet,Umeå centrum för molekylär patogenes (UCMP)
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- Öhman, Anders (author)
- Umeå universitet,Umeå centrum för molekylär patogenes (UCMP)
- (creator_code:org_t)
- Elsevier, 2009
- 2009
- English.
- In: Analytical Biochemistry. - : Elsevier. - 0003-2697 .- 1096-0309. ; 385:2, s. 374-376
- Journal article (peer-reviewed)
Abstract
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- A general method to explore the dynamic nature of amyloid fibrils is described, combining hydrogen/deuterium exchange and nuclear magnetic resonance spectroscopy to determine the exchange rates of individual amide protons within an amyloid fibril. Our method was applied to fibrils formed by the amyloid-beta(1-40) peptide, the major protein component of amyloid plaques in Alzheimer's disease. The fastest exchange rates were detected among the first 14 residues of the peptide, a stretch known to be poorly structured within the fibril. Considerably slower exchange rates were observed in the remainder of the peptide within the beta-strand-turn-beta-strand motif that constitutes the fibrillar core.
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