Peptide folding and aggregation studied using a simplified atomic model
(2005) In Journal of Physics: Condensed Matter 17(18). p.1553-1564- Abstract
- Using an atomic model with a simplified-sequence-based potential, the folding properties of several different peptides are studied. Both alpha-helical (Trp cage, F-s) and beta-sheet(GB1p, GB1m2, GB1m3, Betanova, LLM) peptides are considered. The model is able to fold these different peptides for one and the same choice of;parameters, and the melting behaviour of the peptides (folded population against temperature) is in very good agreement with experimental data. Furthermore, using the same model with unchanged parameters, the aggregation behaviour of a fibril-forming fragment of the Alzheimer's A beta peptide is studied, with very promising results.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/237392
- author
- Irbäck, Anders LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Physics: Condensed Matter
- volume
- 17
- issue
- 18
- pages
- 1553 - 1564
- publisher
- IOP Publishing
- external identifiers
-
- wos:000229658500013
- scopus:24144445368
- ISSN
- 1361-648X
- DOI
- 10.1088/0953-8984/17/18/012
- language
- English
- LU publication?
- yes
- id
- d469dc25-a084-4fcb-a065-e47ca75c662d (old id 237392)
- date added to LUP
- 2016-04-01 16:41:13
- date last changed
- 2024-01-11 12:45:57
@article{d469dc25-a084-4fcb-a065-e47ca75c662d, abstract = {{Using an atomic model with a simplified-sequence-based potential, the folding properties of several different peptides are studied. Both alpha-helical (Trp cage, F-s) and beta-sheet(GB1p, GB1m2, GB1m3, Betanova, LLM) peptides are considered. The model is able to fold these different peptides for one and the same choice of;parameters, and the melting behaviour of the peptides (folded population against temperature) is in very good agreement with experimental data. Furthermore, using the same model with unchanged parameters, the aggregation behaviour of a fibril-forming fragment of the Alzheimer's A beta peptide is studied, with very promising results.}}, author = {{Irbäck, Anders}}, issn = {{1361-648X}}, language = {{eng}}, number = {{18}}, pages = {{1553--1564}}, publisher = {{IOP Publishing}}, series = {{Journal of Physics: Condensed Matter}}, title = {{Peptide folding and aggregation studied using a simplified atomic model}}, url = {{http://dx.doi.org/10.1088/0953-8984/17/18/012}}, doi = {{10.1088/0953-8984/17/18/012}}, volume = {{17}}, year = {{2005}}, }