title: Unconstrained homooligomeric γ-peptides show high propensity for C14 helix formation.
abstract: Monosubstituted γ(4)-residues (γ(4)Leu, γ(4)Ile, and γ(4)Val) form helices even in short homooligomeric sequences. C14 helix formation is established by X-ray diffraction in homooligomeric (γ)n tetra-, hexa- and decapeptide sequences demonstrating the high propensity of γ residues, with proteinogenic side chains, to adopt locally folded conformations.
authors.affiliation: Molecular Biophysics Unit, Department of Physics, Sophisticated Instrumentation Facility, Indian Institute of Science , Bangalore 560 012, India.
authors.forename: Krishnayan
authors.initials: K
authors.lastname: Basuroy
authors.forename: Bhimareddy
authors.initials: B
authors.lastname: Dinesh
authors.forename: M B Madhusudana
authors.initials: MB
authors.lastname: Reddy
authors.forename: Siddapa
authors.initials: S
authors.lastname: Chandrappa
authors.forename: Srinivasarao
authors.initials: S
authors.lastname: Raghothama
authors.forename: Narayanaswamy
authors.initials: N
authors.lastname: Shamala
authors.forename: Padmanabhan
authors.initials: P
authors.lastname: Balaram
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides