Conformational properties of surfactant-like peptides with variable glycine tails
The three-dimensional structures of surfactant-like peptides containing 4–10 glycines as the components of the hydrophobic tails and aspartic acids as the hydrophilic heads (G4D2, G6D2, G8D2, G10D2) are investigated by using the multicanonical simulation procedure. The thermodynamically most stable low energy structures of the sequences are determined. Ramachandran plots are prepared and analyzed to predict the secondary structure motifs of the molecules.
Year of publication: |
2010
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Authors: | Arkın, Handan |
Published in: |
Physica A: Statistical Mechanics and its Applications. - Elsevier, ISSN 0378-4371. - Vol. 389.2010, 2, p. 265-272
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Publisher: |
Elsevier |
Subject: | Molecular modeling | Surfactant-like peptides | Multicanonical simulation | Ramachandran plot |
Saved in:
Online Resource
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