Ang, ShirleyKogulanathan, JanaMorris, Gordon A.Kök, Mehmet ŞamilShewry, Peter R.2021-06-232021-06-2320100175-75711432-1017https://doi.org/10.1007/s00249-009-0529-7https://hdl.handle.net/20.500.12491/6791A 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 similar to 10 to 30 with alpha appearing the most extended and gamma the least.eninfo:eu-repo/semantics/openAccessGliadinSedimentation CoefficientMolecular WeightHeterogeneityAxial RatioExtended ConformationArticle10.1007/s00249-009-0529-7392255261196691332-s2.0-73649091124Q3WOS:000272868600005Q3