title: Novel helical foldamers: organized heterogeneous backbone folding in 1 : 1 alpha/nucleoside-derived-beta-amino acid sequences.
abstract: Secondary structural conformation of hybrid oligo-peptides comprised of 1 : 1 alternating Nucleoside Derived beta-Amino acid (NDA) and l-amino acid residues has been reported. The studies reveal that the NDA residues organize the heterogeneous backbone featuring the surface properties of both nucleic acids and peptides, to adopt a novel 11/8-helical fold.
authors: Organic Division-I, Indian Institute of Chemical Technology (CSIR), Uppal Road, Tarnaka, Hyderabad-500 607 (AP), India. srivaric@iict.res.in
authors: Srivari
authors: S
authors: Chandrasekhar
authors: Nayani
authors: N
authors: Kiranmai
authors: Marelli Udaya
authors: MU
authors: Kiran
authors: Ambure Sharada
authors: AS
authors: Devi
authors: Gangireddy Pavan Kumar
authors: GP
authors: Reddy
authors: Mohammed
authors: M
authors: Idris
authors: Bharatam
authors: B
authors: Jagadeesh
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D008968:Molecular Conformation; D056004:Molecular Dynamics Simulation; D009705:Nucleosides / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry*; D017510:Protein Folding
chemical_list: D000596:Amino Acids; D009705:Nucleosides; D009842:Oligopeptides