Geometrical principles of homomeric β-barrels and β-helices: Application to modeling amyloid protofilaments
- Submitting institution
-
The University of East Anglia
- Unit of assessment
- 11 - Computer Science and Informatics
- Output identifier
- 182621207
- Type
- D - Journal article
- DOI
-
10.1002/prot.25341
- Title of journal
- Proteins: Structure, Function, and Bioinformatics
- Article number
- -
- First page
- 1866
- Volume
- 85
- Issue
- 10
- ISSN
- 0887-3585
- Open access status
- Compliant
- Month of publication
- October
- Year of publication
- 2017
- URL
-
-
- 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
- 2
- Proposed double-weighted
- No
- Reserve for an output with double weighting
- No
- Additional information
- This cover article for Proteins Vol85(10) presents fundamental equations that allow conversion between measureable quantities related to basic helical structures found in proteins, β-helices and β-barrels. The work unifies these two structures locating them at two ends of a whole spectrum. Amyloid is a misfolded form of protein that is known to be involved in diseases such as Alzheimer’s and the equations were used to model the misfolded forms of Alzheimer Aβ protein and transthyretin as a new kind of structure, a “β-strip helix”, that combines qualities of both β-helices and β-barrels.
- Author contribution statement
- -
- Non-English
- No
- English abstract
- -