title: Orthanilic acid-promoted reverse turn formation in peptides.
abstract: Orthanilic acid (2-aminobenzenesulfonic acid, (S)Ant), an aromatic β-amino acid, has been shown to be highly useful in inducing a folded conformation in peptides. When incorporated into peptide sequences (Xaa-(S)Ant-Yaa), this rigid aromatic β-amino acid strongly imparts a reverse-turn conformation to the peptide backbone, featuring robust 11-membered-ring hydrogen-bonding.
authors: Division of Organic Chemistry, National Chemical Laboratory, Dr Homi Bhabha Road, Pune 411 008, India.
authors: Sangram S
authors: SS
authors: Kale
authors: Gowri
authors: G
authors: Priya
authors: Amol S
authors: AS
authors: Kotmale
authors: Rupesh L
authors: RL
authors: Gawade
authors: Vedavati G
authors: VG
authors: Puranik
authors: P R
authors: PR
authors: Rajamohanan
authors: Gangadhar J
authors: GJ
authors: Sanjayan
mesh_terms: D006860:Hydrogen Bonding; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D013425:Sulfanilic Acids / Q000737:chemistry*
chemical_list: D010455:Peptides; D013425:Sulfanilic Acids; C100048:2-sulfanilic acid