title: Concurrent display of both α- and β-turns in a model peptide.
abstract: This article describes a model peptide that concurrently displays both α- and β-turns, as demonstrated by structural investigations using single crystal X-ray crystallography and solution-state NMR studies. The motif reported herein has the potential for the design of novel conformationally ordered synthetic oligomers with structural architectures distinct from those classically observed.
authors: Division of Organic Chemistry, National Chemical Laboratory, Pune, India.
authors: Deekonda
authors: D
authors: Srinivas
authors: Kuruppanthara N
authors: KN
authors: Vijayadas
authors: Rajesh
authors: R
authors: Gonnade
authors: Usha D
authors: UD
authors: Phalgune
authors: Pattuparambil R
authors: PR
authors: Rajamohanan
authors: Gangadhar J
authors: GJ
authors: Sanjayan
mesh_terms: D020816:Amino Acid Motifs; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides