title: Peptoid helicity modulation: precise control of peptoid secondary structures via position-specific placement of chiral monomers.
abstract: The degree of peptoid helicity can be effectively modulated by position-specific incorporation of α-chiral aromatic monomers. In this study, we report the structural role of each monomer position collected from 30 comprehensive model peptoid oligomers demonstrating a meticulous manner to fine-tune peptoid secondary structures.
authors.affiliation: School of Materials Science and Engineering, Gwangju Institute of Science and Technology, Gwangju, 500-712, Republic of Korea. mhyoon@gist.ac.kr.
authors.forename: Hye-Min
authors.initials: HM
authors.lastname: Shin
authors.forename: Chang-Muk
authors.initials: CM
authors.lastname: Kang
authors.forename: Myung-Han
authors.initials: MH
authors.lastname: Yoon
authors.forename: Jiwon
authors.initials: J
authors.lastname: Seo
mesh_terms: D001596:Benzylamines / Q000737:chemistry; D002942:Circular Dichroism; D008968:Molecular Conformation; D034444:Peptoids / Q000737:chemistry*; D010627:Phenethylamines / Q000737:chemistry; D013237:Stereoisomerism
chemical_list: D001596:Benzylamines; D034444:Peptoids; D010627:Phenethylamines; C030796:benzylamine