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Promotion of Folding in Hybrid Peptides through Unconstrained γ Residues: Structural Characterization of Helices in (αγγ) n and (αγα) n Sequences
Author(s) -
Basuroy Krishnayan,
Dinesh Bhimareddy,
Shamala Narayanaswamy,
Balaram Padmanabhan
Publication year - 2013
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.201209324
Subject(s) - residue (chemistry) , folding (dsp implementation) , hydrogen bond , helix (gastropod) , crystallography , protein folding , sequence (biology) , chemistry , stereochemistry , peptide sequence , amino acid residue , molecule , biochemistry , biology , gene , ecology , organic chemistry , snail , electrical engineering , engineering
The γ‐amino acid residue γ 4 (R)Val promotes helical folding even in short (αγα) n sequences. A mixed C 12 /C 14 helix (in which hydrogen bonds close a ring of 12 or 14 atoms) is established in a 12‐residue (αγγ) 4 sequence (see picture, right). The 6‐residue (αγα) 2 sequence (left), devoid of backbone conformational constraints, folds into a C 12 /C 10 helix.