title: Distinctive circular dichroism signature for 14-helix-bundle formation by beta-peptides.
abstract: We identify a distinctive circular dichroism (CD) signature for self-assembled 14-helical beta-peptides. Our data show that self-assembly leads to a mimimum at 205 nm, which is distinct from the well-known minimum at 214 nm for a monomeric 14-helix. The onset of assembly is indicated by [theta]205/[theta]214>0.7. Our results will facilitate rapid screening for self-assembling beta-peptides and raise the possibility that far-UV CD will be useful for detecting higher-order structure for other well-folded oligoamide backbones.
authors.affiliation: Department of Chemistry, University of Wisconsin, Madison, WI 53706, USA.
authors.forename: William C
authors.initials: WC
authors.lastname: Pomerantz
authors.forename: Tami L R
authors.initials: TL
authors.lastname: Grygiel
authors.forename: Jonathan R
authors.initials: JR
authors.lastname: Lai
authors.forename: Samuel H
authors.initials: SH
authors.lastname: Gellman
mesh_terms: D002942:Circular Dichroism; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides