Multi-strand β-sheet of Alzheimer Aβ(1-40) folds to β-strip helix: Implication for protofilament formation
- Submitting institution
-
The University of East Anglia
- Unit of assessment
- 11 - Computer Science and Informatics
- Output identifier
- 182621678
- Type
- D - Journal article
- DOI
-
10.1080/07391102.2018.1477626
- Title of journal
- Journal of Biomolecular Structure and Dynamics
- Article number
- -
- First page
- 2143
- Volume
- 37
- Issue
- 8
- ISSN
- 0739-1102
- Open access status
- Compliant
- Month of publication
- May
- Year of publication
- 2019
- URL
-
http://www.scopus.com/inward/record.url?scp=85058154467&partnerID=8YFLogxK
- Supplementary information
-
-
- Request cross-referral to
- -
- Output has been delayed by COVID-19
- No
- COVID-19 affected output statement
- -
- Forensic science
- No
- Criminology
- No
- Interdisciplinary
- Yes
- Number of additional authors
-
1
- Research group(s)
-
-
- Citation count
- 0
- Proposed double-weighted
- No
- Reserve for an output with double weighting
- No
- Additional information
- This paper presents the results of large-scale Molecular Dynamics simulations (partly performed on the K-Computer, Japan’s foremost supercomputer at the time) on the Alzheimer Aβ protein. It is based on the result of fundamental work by Hayward and Milner-White (“Geometrical Principles of Homomeric β‐barrels and β‐helices: Application to Modelling Amyloid Protofilaments”, Proteins, 85 (10) October 2017). Hayward and Kitao were awarded a Tokyo Institute of Technology “Research Abroad and Invitational for International Collaboration” grant in July 2018 to develop further their work in this area by simulating familial mutants of the Aβ protein. A paper is in preparation.
- Author contribution statement
- -
- Non-English
- No
- English abstract
- -