title: Helical folding in heterogeneous foldamers without inter-residual backbone hydrogen-bonding.
abstract: This communication describes a set of hybrid foldamers that do not feature inter-residual, but intra-residual backbone hydrogen-bonding, yet adopt a preferentially folded conformation displaying right-handed helical architecture. Conformational ordering is apparently due to the combined conformational restrictions imposed by the conformationally restricted individual amino acid residues with which the oligomers are made of.
authors: Division of Organic Synthesis, National Chemical Laboratory, Dr Homi Bhabha Road, Pune 411 008, India.
authors: Gowri
authors: G
authors: Priya
authors: Amol S
authors: AS
authors: Kotmale
authors: Rupesh L
authors: RL
authors: Gawade
authors: Deepti
authors: D
authors: Mishra
authors: Sourav
authors: S
authors: Pal
authors: Vedavadi G
authors: VG
authors: Puranik
authors: Pattuparambil R
authors: PR
authors: Rajamohanan
authors: Gangadhar J
authors: GJ
authors: Sanjayan
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D002264:Carboxylic Acids / Q000737:chemistry; D018360:Crystallography, X-Ray; D006859:Hydrogen / Q000737:chemistry; D006860:Hydrogen Bonding; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013876:Thiophenes / Q000737:chemistry
chemical_list: D000596:Amino Acids; D002264:Carboxylic Acids; D010455:Peptides; D013876:Thiophenes; D006859:Hydrogen