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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 30, Number 3
BKCSDE 30(3)
March 20, 2009 

Structural Properties of Fibril-forming Segments of α-Synuclein
Jeseong Yoon, Joonho Park, Soonmin Jang, Kyunghee Lee, Seokmin Shin*
Replica-exchange molecular dynamics, Fibril formation, α-Synuclein, Natively unstructured protein, Representative structure
We have performed replica-exchange molecular dynamics simulations on 41 residue peptide mainly composed of NAC (non Aβ component) sequence in α-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 α-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.
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