title: Structure and heterogeneity of gliadin: a hydrodynamic evaluation.
abstract: 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.
authors: NCMH Laboratory, Division of Food Science, School of Biosciences, National Centre for Macromolecular Hydrodynamics (NCMH), University of Nottingham, Sutton Bonington, LE12 5RD, UK.
authors: Shirley
authors: S
authors: Ang
authors: Jana
authors: J
authors: Kogulanathan
authors: Gordon A
authors: GA
authors: Morris
authors: M Samil
authors: MS
authors: Kök
authors: Peter R
authors: PR
authors: Shewry
authors: Arthur S
authors: AS
authors: Tatham
authors: Gary G
authors: GG
authors: Adams
authors: Arthur J
authors: AJ
authors: Rowe
authors: Stephen E
authors: SE
authors: Harding
mesh_terms: 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
chemical_list: D014867:Water; D005903:Gliadin