N-versus C-terminal control over the screw-sense preference of the configurationally achiral, conformationally helical peptide motif Aib(8)GlyAib(8).
Conformational control over the screw sense of a helical 17-mer of achiral amino acids, Aib(8)GlyAib(8), 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(8)GlyAib(8) forms the longest 3(10) helical structure observed crystallographically to date.
School of Chemistry, University of Manchester, Oxford Road, Manchester M13 9PL, UK.
Jordi
J
Solà
Madeleine
M
Helliwell
Jonathan
J
Clayden
D000621:Aminoisobutyric Acids / Q000737:chemistry*; D018360:Crystallography, X-Ray; D005998:Glycine / Q000737:chemistry*; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation
D000621:Aminoisobutyric Acids; D010455:Peptides; D005998:Glycine