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- Title
Promotion of Folding in Hybrid Peptides through Unconstrained γ Residues: Structural Characterization of Helices in (αγγ)<sub> n</sub> and (αγα)<sub> n</sub> Sequences.
- Authors
Basuroy, Krishnayan; Dinesh, Bhimareddy; Shamala, Narayanaswamy; Balaram, Padmanabhan
- Abstract
The γ‐amino acid residue γ4(R)Val promotes helical folding even in short (αγα)n sequences. A mixed C12/C14 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 C12/C10 helix.
- Publication
Angewandte Chemie International Edition, 2013, Vol 52, Issue 11, p3136
- ISSN
1433-7851
- Publication type
Article
- DOI
10.1002/anie.201209324