title: Origins of the high 14-helix propensity of cyclohexyl-rigidified residues in beta-peptides.
abstract: [structure: see text] beta-Peptides containing residues derived from trans-2-aminocyclohexanecarboxylic acid (ACHC) display high population of 14-helical secondary structure in aqueous solution. We show that hydrophobic interactions between cyclohexyl rings are not responsible for this conformation-promoting effect, and that polar groups may be attached to the cyclohexyl ring without diminishing the effect.
authors: Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
authors: Myung-Ryul
authors: MR
authors: Lee
authors: Tami L
authors: TL
authors: Raguse
authors: Marina
authors: M
authors: Schinnerl
authors: William C
authors: WC
authors: Pomerantz
authors: Xiaodong
authors: X
authors: Wang
authors: Peter
authors: P
authors: Wipf
authors: Samuel H
authors: SH
authors: Gellman
mesh_terms: D002942:Circular Dichroism; D003500:Cyclization; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides