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Krishnayan Basuroy, Bhimareddy Dinesh, Prof. Narayanaswamy Shamala and Prof. Padmanabhan Balaram Promotion of Folding in Hybrid Peptides through Unconstrained γ Residues: Structural Characterization of Helices in (αγγ)n and (αγα)n Sequences Angewandte Chemie International Edition 52

Version of Record online: 4 FEB 2013 | DOI: 10.1002/anie.201209324

Thumbnail image of graphical 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.

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