Multicanonical Monte Carlo simulations of a de novo designed protein with end-to-end beta-sheet
Küçük Resim Yok
Tarih
2014
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Amer Inst Physics
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
One of the smallest proteins with end-to-end beta-sheet is the designed 36-residue protein DS119. We recently suggested that the rate-limiting step in the folding of the beta alpha beta protein is the formation of the central helix that then provides a scaffold for the parallel beta-sheet formed by the two chain ends. In the present report we investigate whether and how this folding mechanism depends on the energy function, and compare the efficiency of molecular dynamics and Monte Carlo implementations of multicanonical sampling. While we find the native structure with similar frequency as in our previous simulations, we observe that the folding mechanism differs for both force fields. (C) 2014 AIP Publishing LLC.
Açıklama
PubMed ID: 24527937
Anahtar Kelimeler
Kaynak
Journal of Chemical Physics
WoS Q Değeri
Q1
Scopus Q Değeri
Q1
Cilt
140
Sayı
6
