Secondary structure prediction of beta-hairpin peptide tryptophan zipper-I
Küçük Resim Yok
Tarih
2008
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Elsevier Science Bv
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
We have investigated the folding properties of tryptophan zipper-I molecule which folds into a stable beta-hairpin motif in aqueous solution as suggested by nuclear magnetic resonance (NMR) experiments. An all-atom presentation, including hydrogen, was used with an implicit solvent. As a simulation technique, simulated tempering algorithm was used to obtain equilibrium conformations of the molecule at ten distinct temperatures. Our minimum energy configuration obtained from simulated tempering algorithm is a beta-hairpin motif with 1.30 angstrom backbone root-mean-square deviation from the reference PDB structure (11e0.pdb). Several quantities and exhaustive folding free energy landscapes were determined and discussed in order to clarify the folding behavior. (c) 2008 Elsevier B.V. All rights reserved.
Açıklama
Anahtar Kelimeler
tryptophan zipper, beta-hairpin, generalized ensembles, simulated tempering
Kaynak
Physica A-Statistical Mechanics and Its Applications
WoS Q Değeri
Q2
Scopus Q Değeri
Q2
Cilt
387
Sayı
14
