Structural Properties of Fibril-forming Segments of alpha-Synuclein

Cited 1 time in webofscience Cited 0 time in scopus
  • Hit : 68
  • Download : 0
We have performed replica-exchange molecular dynamics simulations on 41 residue peptide mainly composed of NAC (non A beta component) sequence in alpha-Synuclein. To investigate conformational characteristics of intrinsically unstructured peptides, we carried out structural analysis on the 'representative structures' for ensemble of structures occurring at different temperatures. The secondary structure profile obtained from our simulations suggests that the NAC region of alpha-synuclein can be divided into roughly three helical-like segments. It is found that the overall helix-turn-helix like topology is conserved even though the conformational fluctuations grow as the temperature increases. The coordinate-based and the distance-based representative structures exhibit noticeable differences at higher temperatures while they are similar at lower temperatures. It is found that structural variations for the coordinate-based representative structures are much larger, suggesting that distance-based representative structures provide more reliable information concerning characteristic features of intrinsically unstructured proteins. The present analysis also indicates that the conformational features of representative structures at high temperatures might be related to those in membrane or low pH environment.
Publisher
WILEY-V C H VERLAG GMBH
Issue Date
2009-03
Language
English
Article Type
Article
Citation

BULLETIN OF THE KOREAN CHEMICAL SOCIETY, v.30, no.3, pp.623 - 629

ISSN
0253-2964
URI
http://hdl.handle.net/10203/286127
Appears in Collection
EEW-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 1 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0