Structure and heterogeneity of gliadin: A hydrodynamic evaluation

Shirley Ang; Jana Kogulanathan; Gordon A. Morris; M. Samil Kök; Peter R. Shewry; Arthur S. Tatham; Gary G. Adams; Arthur J. Rowe; Stephen E. Harding

doi:10.1007/s00249-009-0529-7

Structure and heterogeneity of gliadin: A hydrodynamic evaluation

Shirley Ang, Jana Kogulanathan, Gordon A. Morris, M. Samil Kök, Peter R. Shewry, Arthur S. Tatham, Gary G. Adams, Arthur J. Rowe, Stephen E. Harding

Research output: Contribution to journal › Article › peer-review

41 Citations (Scopus)

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 (α, γ, ω_slow, ω_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 α appearing the most extended and γ the least.

Original language	English
Pages (from-to)	255-261
Number of pages	7
Journal	European Biophysics Journal
Volume	39
Issue number	2
Early online date	8 Aug 2009
DOIs	https://doi.org/10.1007/s00249-009-0529-7
Publication status	Published - Jan 2010
Externally published	Yes

Access to Document

10.1007/s00249-009-0529-7Licence: Unspecified

Cite this

@article{138dfacdc9914ad79fbda4d373ff86a6,

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 (α, γ, ωslow, ωfast) 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 α appearing the most extended and γ the least.",

keywords = "Axial ratio, Extended conformation, Gliadin, Heterogeneity, Molecular weight, Sedimentation coefficient",

author = "Shirley Ang and Jana Kogulanathan and Morris, {Gordon A.} and K{\"o}k, {M. Samil} and Shewry, {Peter R.} and Tatham, {Arthur S.} and Adams, {Gary G.} and Rowe, {Arthur J.} and Harding, {Stephen E.}",

year = "2010",

month = jan,

doi = "10.1007/s00249-009-0529-7",

language = "English",

volume = "39",

pages = "255--261",

journal = "European Biophysics Journal",

issn = "0175-7571",

publisher = "Springer Verlag",

number = "2",

}

TY - JOUR

T1 - Structure and heterogeneity of gliadin

T2 - A hydrodynamic evaluation

AU - Ang, Shirley

AU - Kogulanathan, Jana

AU - Morris, Gordon A.

AU - Kök, M. Samil

AU - Shewry, Peter R.

AU - Tatham, Arthur S.

AU - Adams, Gary G.

AU - Rowe, Arthur J.

AU - Harding, Stephen E.

PY - 2010/1

Y1 - 2010/1

N2 - 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 (α, γ, ωslow, ωfast) 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 α appearing the most extended and γ the least.

AB - 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 (α, γ, ωslow, ωfast) 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 α appearing the most extended and γ the least.

KW - Axial ratio

KW - Extended conformation

KW - Gliadin

KW - Heterogeneity

KW - Molecular weight

KW - Sedimentation coefficient

UR - http://www.scopus.com/inward/record.url?scp=73649091124&partnerID=8YFLogxK

UR - https://link.springer.com/journal/249

U2 - 10.1007/s00249-009-0529-7

DO - 10.1007/s00249-009-0529-7

M3 - Article

C2 - 19669133

AN - SCOPUS:73649091124

VL - 39

SP - 255

EP - 261

JO - European Biophysics Journal

JF - European Biophysics Journal

SN - 0175-7571

IS - 2

ER -

Structure and heterogeneity of gliadin: A hydrodynamic evaluation

Abstract

Access to Document

Other files and links

Fingerprint

Cite this