Helices and other secondary structures of β- and γ-peptides
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Date
2006
Publication Type
Review Article
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yes
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Abstract
The principal secondary structural motifs adopted by peptides assembled from β‐amino acid units are discussed: the 14‐, 12‐, 10‐, 12/10‐, and 8‐helices, as well as the hairpin turn, extended structures, stacks, and sheets. Features that promote a particular folding propensity are outlined and illustrated by structures determined in solution (NMR) and in the solid‐state (x‐ray). The N–Cβ–Cα–CO dihedral angles from molecular dynamics simulations, which are indicative of a particular secondary structure, are presented. A brief description of a helix and a turn of γ‐peptides is also given. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 23–37, 2006
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published
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Journal / series
Volume
84 (1)
Pages / Article No.
23 - 37
Publisher
Wiley-Blackwell
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Date created
Subject
β-amino acid; conformational analysis; GROMOS simulation package; hairpin turn; helix; molecular dynamics simulation; NMR; β-peptide; γ-peptide; secondary structure; torsion angle
Organisational unit
03492 - Hilvert, Donald (emeritus) / Hilvert, Donald (emeritus)
03304 - Van Gunsteren, Wilfred F. (emeritus)
Notes
Received 1 September 2005, Revised 4 October 2005, Accepted 10 October 2005, Published Online 18 October 2005.