Structure and heterogeneity of gliadin: a hydrodynamic evaluation.
A study of the heterogeneity and conformation in solution [in 70% (v/v) aq. ethanol] of gliadin proteins from wheat was undertaken based upon sedimentation velocity in the analytical ultracentrifuge, analysis of the distribution coefficients and ellipsoidal axial ratios assuming quasi-rigid particles, allowing for a range of plausible time-averaged hydration values. All classical fractions (alpha, gamma, omega(slow), omega(fast)) show three clearly resolved components. Based on the weight-average sedimentation coefficient for each fraction and a weight-average molecular weight from sedimentation equilibrium and/or cDNA sequence analysis, all the proteins are extended molecules with axial ratios ranging from ~10 to 30 with alpha appearing the most extended and gamma the least.
Ang
Shirley
S
NCMH Laboratory, Division of Food Science, School of Biosciences, National Centre for Macromolecular Hydrodynamics (NCMH), University of Nottingham, Sutton Bonington, LE12 5RD, UK.
Kogulanathan
Jana
J
Morris
Gordon A
GA
Kök
M Samil
MS
Shewry
Peter R
PR
Tatham
Arthur S
AS
Adams
Gary G
GG
Rowe
Arthur J
AJ
Harding
Stephen E
SE
D000465:Algorithms; D018740:Genetic Heterogeneity; D005903:Gliadin / Q000737:chemistry* / Q000235:genetics*; D008970:Molecular Weight; D009038:Motion; D011487:Protein Conformation; D017422:Sequence Analysis, DNA; D013997:Time Factors; D014908:Triticum; D014461:Ultracentrifugation; D014867:Water / Q000737:chemistry
D014867:Water; D005903:Gliadin