title: Secondary structures of narcissus mosaic virus coat protein.
abstract: Circular dichroism (CD) measurements on the coat protein of narcissus mosaic virus particles show that the dominant secondary structure is the alpha-helix, with a 45 (+/- 2)% content. The beta-sheet content is much lower at 5 (+/- 3)%. Both values are essentially the same as those found in potato virus X coat protein. The CD results are used to assess the results of secondary structure prediction methods.
authors.affiliation: Department of Biological and Molecular Sciences, University of Stirling.
authors.forename: H R
authors.initials: HR
authors.lastname: Wilson
authors.forename: P
authors.initials: P
authors.lastname: Tollin
authors.forename: L
authors.initials: L
authors.lastname: Sawyer
authors.forename: D J
authors.initials: DJ
authors.lastname: Robinson
authors.forename: N C
authors.initials: NC
authors.lastname: Price
authors.forename: S M
authors.initials: SM
authors.lastname: Kelly
mesh_terms: D002213:Capsid / Q000737:chemistry*; D002942:Circular Dichroism; D009029:Mosaic Viruses / Q000032:analysis*; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D014961:X-Ray Diffraction / Q000379:methods