Helix packing of leucine‐rich peptides: A parallel leucine ladder in the structure of Boc‐Aib‐Leu‐Aib‐Aib‐Leu‐Leu‐Leu‐Aib‐Leu‐Aib‐OMe
Copyright policy )Helix packing of leucine‐rich peptides: A parallel leucine ladder in the structure of Boc‐Aib‐Leu‐Aib‐Aib‐Leu‐Leu‐Leu‐Aib‐Leu‐Aib‐OMe
AbstractThe packing of peptide helices in crystals of the leucine‐rich decapeptide Boc‐Aib‐Leu‐Aib‐Aib‐Leu‐Leu‐Leu‐Aib‐Leu‐Aib‐OMe provides an example of ladder‐like leucylleucyl interactions between neighboring molecules. The peptide molecule forms a helix with five 5→1 hydrogen bonds and two 4→1 hydrogen bonds near the C terminus. Three head‐to‐tail NH ċ O = C hydrogen bonds between helices form continuous columns of helices in the crystal. The helicial columns associate in an antiparallel fashion, except for the association of Leu ċ Leu side chains, which occurs along the diagonal of the cell where the peptide helices are parallel. The peptide, with formula C56H102N10O13, crystallizes in space group P212121 with Z = 4 and cell parameters a = 16.774(3) Å, b = 20.032(3) Å and c = 20.117(3) Å; overall agreement factor R = 10.7% for 2014 data with |Fobs| < 3σ(F); resolution 1.0 Å.
- Indian Institute of Science Bangalore India
- Naval Research Laboratory Optical Sciences Division United States
- United States Naval Research Laboratory United States
Models, Molecular, Leucine, Protein Conformation, Molecular Sequence Data, 500, Hydrogen Bonding, Amino Acid Sequence, Molecular Biophysics Unit, 540, Oligopeptides
Models, Molecular, Leucine, Protein Conformation, Molecular Sequence Data, 500, Hydrogen Bonding, Amino Acid Sequence, Molecular Biophysics Unit, 540, Oligopeptides
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