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Characteristic Structural Parameters for the γ‐Peptide 14‐Helix: Importance of Subunit Preorganization
Author(s) -
Guo Li,
Zhang Weicheng,
Reidenbach Andrew G.,
Giuliano Michael W.,
Guzei Ilia A.,
Spencer Lara C.,
Gellman Samuel H.
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201101301
Subject(s) - peptide , folding (dsp implementation) , helix (gastropod) , substitution (logic) , crystallography , protein subunit , chemistry , set (abstract data type) , computational biology , residue (chemistry) , computer science , stereochemistry , biochemistry , biology , engineering , programming language , gene , ecology , snail , electrical engineering
All wound up : Crystallographic data for a set of homologous peptides constructed from gabapentin and two to six preorganized γ‐amino acid residues (see crystal structure of the longest peptide) allow derivation of characteristic parameters for the γ‐peptide 14‐helix and establish guidelines for characterizing 14‐helical folding. The results suggest that the substitution pattern of a γ‐residue has a profound effect on the propensity for 14‐helical folding.