title: Circular dichroism studies of distorted alpha-helices, twisted beta-sheets, and beta turns.
abstract: Theoretical models for calculating the circular dichroism (CD) of biopolymers have been constructed which allow the evaluation of the effects of geometric distortions within regular secondary structures. Outward tilting of the carbonyl group within alpha-helical structures yields calculated CD spectra with diminished intensity and a red-shifted maximum near 190 nm. The alpha II-helix provides an extreme example of this type of alpha-helix distortion. It is predicted that a mixture of alpha and alpha II structures in bacteriorhodopsin can account for its anomalous CD spectrum. The minimum length of alpha-helix required to produce an alpha-helix-like CD spectrum is calculated to be two to three turns (seven to eleven residues), while helices greater than 30 residues should provide adequate models of an infinite helix. Twisting of beta-sheets is predicted to lead to an increase in CD intensity and significant shifts in band position. Calculated CD spectra for beta-turn models are accurate for types II and II', but appear to be inadequate for type I turns.
authors.affiliation: Department of Biochemistry, Colorado State University, Fort Collins 80523.
authors.forename: M C
authors.initials: MC
authors.lastname: Manning
authors.forename: M
authors.initials: M
authors.lastname: Illangasekare
authors.forename: R W
authors.initials: RW
authors.lastname: Woody
mesh_terms: D002942:Circular Dichroism; D011487:Protein Conformation; D011506:Proteins; D013329:Structure-Activity Relationship
chemical_list: D011506:Proteins