Solution conformational analysis of the alpha-zein proteins of maize.
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.
Tatham
A S
AS
Department of Agricultural Sciences, University of Bristol, United Kingdom.
Field
J M
JM
Morris
V J
VJ
I'Anson
K J
KJ
Cardle
L
L
Dufton
M J
MJ
Shewry
P R
PR
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*
D012996:Solutions; D015028:Zein