The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Amyloid β‐protein monomer structure: A computational and experimental study
Open accessAbstract
The structural properties of the Aβ42 peptide, a main constituent of the amyloid plaques formed in Alzheimer's disease, were investigated through a combination of ion‐mobility mass spectrometry and theoretical modeling. Replica exchange molecular dynamics simulations using a fully atomic description of the peptide and implicit water solvent were performed on the −3 charge state of the peptide, its preferred state under experimental conditions. Equilibrated structures at 300 K were clustered into three distinct families with similar structural features within a family and with significant root mean square deviations between families. An analysis of secondary structure indicates the Aβ42 peptide conformations are dominated by loops and turns but show some helical structure in the C‐terminal hydrophobic tail. A second calculation on Aβ42 in a solvent‐free environment yields compact structures turned “inside out” from the solution structures (hydrophobic parts on the outside, polar parts on the inside). Ion mobility experiments on the Aβ42 −3 charge state electrosprayed from solution yield a bimodal arrival time distribution. This distribution can be quantitatively fit using cross‐sections from dehydrated forms of the three families of calculated solution structures and the calculated solvent‐free family of structures. Implications of the calculations on the early stages of aggregation of Aβ42 are discussed.
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Cites
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Cited by
The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
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Self-citationProtein misfolding and aggregation in Alzheimer’s disease and type 2 diabetes mellitus
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Metadata
- Authors
- Baumketner, A., Bernstein, S. L., Wyttenbach, T., Bitan, G., Teplow, D. B., Bowers, M. T., & Shea, J.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2006-03
- Volume
- 15
- Issue
- 3
- Pages
- 420-428
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W1976545437
- Cited by
- 247
- References
- 10
- FWCI
- 10.59
- Type
- journal article
- Language
- en
- Open access
- bronze
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