1219615-82-3Relevant academic research and scientific papers
Interruption of a 310-helix by a single Gly residue in a poly-Aib motif: A crystallographic study
Sola, Jordi,Helliwell, Madeleine,Clayden, Jonathan
, p. 62 - 69 (2012/02/02)
The structural influence of a single Gly residue inserted into an Aib16 homooligomer was studied in the solid state by X-ray crystallography. The peptides N3Aib8GlyAib8PheNH2 (1) and CbzPheAib8/
N- versus C-terminal control over the screw-sense preference of the configurationally achiral, conformationally helical peptide motif Aib 8GlyAib8
Sola, Jordi,Helliwell, Madeleine,Clayden, Jonathan
supporting information; experimental part, p. 4548 - 4549 (2010/06/13)
Conformational control over the screw sense of a helical 17-mer of achiral amino acids, Aib8GlyAib8, from a single chiral residue located at the N-terminus is better than that from a single amino acid located at the C-terminus. X-ray crystallography indicates that Aib 8GlyAib8 forms the longest 310 helical structure observed crystallographically to date.
