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GrainGenes Reference Report: BPY-67-487

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Reference	BPY-67-487
Title	Study of high molecular weight wheat glutenin subunit 1Dx5 by C-13 and H-1 solid-state NMR spectroscopy. I. Role of covalent crosslinking
Journal	Biopolymers
Year	2002
Volume	67
Pages	487-498
Author	Alberti E Gilert SM Tatham AS Shewry PR Gil AM
Abstract	Summary: This work describes a carbon and proton solid-state NMR study of the hydration of a high molecular weight wheat glutenin subunit, 1Dx5. The effect of the presence of disulfide bonds on the hydration behavior of the subunit is investigated by a comparison of the unalkylated and alkylated forms of the protein. Hydration induces partial plasticization of the protein so that some segments become more mobile than others. The 13C cross-polarization and magic-angle spinning (MAS) spectra of the samples in the dry state and at two hydration levels (approximately 40 and approximately 65% D2O) were used to monitor the protein fraction resisting plasticization (trains). Conversely, 13C single pulse excitation and 1H-MAS experiments were used to gain information on the more plasticized segments (loops). The molecular motion of the two protein dynamic populations was further characterized by 13C T1 and 1H T1p, T2, and T1 relaxation times. The results suggest that hydration leads to the formation of a network held by a cooperative action of hydrogen bonded glutamines and some hydrophobic interactions. The looser protein segments are suggested to be glycine- and glutamine-rich segments. The primary structure is therefore expected to significantly determine the proportion of trains and loops in the network. The presence of disulfide bonds was observed to promote easier plasticization of the protein and the formation of a more mobile network, probably involving a higher number of loops and/or larger loops
External Databases	Pubmed: 12209455
Keyword	[ Hide all but 1 of 58 ] angle-spinning method behavior biochemistry biophysics bonds breadmaking quality c-13 c-hordein carbon chemical shifts chemical-shifts conformational characterization cross-polarization crosslinking disulfide bond dynamics formation fraction glutamine glutenin glutenin subunit glycine high molecular weight high molecular weight subunits hydration hydrogen hydrogen bonds hydrophobic interactions information lead leads magic-angle spinning mas molecular weight nmr nmr spectroscopy nmr-spectroscopy plasticization polypeptide primary structure protein protein fraction proton pulse relaxation seed storage protein segment solid state solid-state nmr spectra spectroscopy spectrum state structure subunit wheat glutenin wheat glutenin subunit 1dx5 wheat proteins

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