Journal
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
Volume 39, Issue 2, Pages 255-261Publisher
SPRINGER
DOI: 10.1007/s00249-009-0529-7
Keywords
Gliadin; Sedimentation coefficient; Molecular weight; Heterogeneity; Axial ratio; Extended conformation
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Funding
- Biotechnology and Biological Sciences Research Council of the United Kingdom
- BBSRC [BB/D01364X/1, BBS/E/C/00004953] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D01364X/1, BBS/E/C/00004953] Funding Source: researchfish
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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.
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