title: Solution conformational analysis of the alpha-zein proteins of maize.
abstract: Small angle x-ray scattering and viscometric analyses of the alpha-zeins of maize in solution indicated that the molecules were asymmetric. Structure predictions of consensus sequences for the two classes of alpha-zeins, Z19 and Z22, were in good agreement with the alpha-helical contents determined by circular dichroism. Dimensions determined by small angle x-ray scattering and viscometry indicated a predominantly alpha-helical conformation. The data are discussed in relation to models for the solution conformation and to earlier models for alpha-zeins structure.
authors.affiliation: Department of Agricultural Sciences, University of Bristol, United Kingdom.
authors.forename: A S
authors.initials: AS
authors.lastname: Tatham
authors.forename: J M
authors.initials: JM
authors.lastname: Field
authors.forename: V J
authors.initials: VJ
authors.lastname: Morris
authors.forename: K J
authors.initials: KJ
authors.lastname: I'Anson
authors.forename: L
authors.initials: L
authors.lastname: Cardle
authors.forename: M J
authors.initials: MJ
authors.lastname: Dufton
authors.forename: P R
authors.initials: PR
authors.lastname: Shewry
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012542:Scattering, Radiation; D012996:Solutions; D003313:Zea mays / Q000737:chemistry*; D015028:Zein / Q000737:chemistry*
chemical_list: D012996:Solutions; D015028:Zein