Structure and heterogeneity of gliadin: a hydrodynamic evaluation
Yükleniyor...
Dosyalar
Tarih
2010
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Springer
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
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 similar to 10 to 30 with alpha appearing the most extended and gamma the least.
Açıklama
Anahtar Kelimeler
Gliadin, Sedimentation Coefficient, Molecular Weight, Heterogeneity, Axial Ratio, Extended Conformation
Kaynak
European Biophysics Journal With Biophysics Letters
WoS Q Değeri
Q3
Scopus Q Değeri
Q3
Cilt
39
Sayı
2
