Journal Article

FZJ-2013-02980

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Characterizing the First Steps of Amyloid Formation for the ccβ Peptide

Strodel, B. (Corresponding author)FZJ* ; Fitzpatrick, A. W. ; Vendruscolo, M. ; Dobson, C. M. ; Wales, D. J.

2008
Soc. Washington, DC

This record in other databases:  

Please use a persistent id in citations: doi:10.1021/jp801222x

Abstract: We employ constant-temperature and replica exchange molecular dynamics to survey the free energy landscape of the ccbeta peptide using a united-atom potential and an implicit solvent representation. Starting from the experimental coiled-coil structure we observe alpha to beta conversion on increasing the temperature, in agreement with experiment. Various beta-sheet trimers are identified as free energy minima, including one that closely resembles the amyloid beta-sheet model previously proposed from experimental data. We characterize two alternative pathways leading to beta-sheets. The first proceeds via direct alpha to beta conversion without dissociation of the trimer, and the second can be classified as a dissociation/reassociation pathway.

---

Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 452 - Structural Biology (POF2-452) (POF2-452)

Appears in the scientific report 2013

---

Database coverage:
; Current Contents - Social and Behavioral Sciences ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

---