| Literature DB >> 19669133 |
Shirley Ang1, Jana Kogulanathan, Gordon A Morris, M Samil Kök, Peter R Shewry, Arthur S Tatham, Gary G Adams, Arthur J Rowe, Stephen E Harding.
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.Entities:
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Year: 2009 PMID: 19669133 DOI: 10.1007/s00249-009-0529-7
Source DB: PubMed Journal: Eur Biophys J ISSN: 0175-7571 Impact factor: 1.733