Comparison of Repetitive Sequences Derived from High Molecular Weight Subunits of Wheat Glutenin, an Elastomeric Plant Protein
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- 作者：Nikolaus Wellner ; Justin T. Marsh ; Andrew W. J. Savage ; Nigel G. Halford ; Peter R. Shewry ; E. N. Clare Mills ; and Peter S. Belton
- 刊名：Biomacromolecules
- 出版年：2006
- 出版时间：April 2006
- 年：2006
- 卷：7
- 期：4
- 页码：1096 - 1103
- 全文大小：311K
- 年卷期：v.7,no.4(April 2006)
- ISSN：1526-4602
文摘
A strategy has been developed to create repetitive peptides incorporating substitutions in the PGQGQQGYYPTSLQQconsensus repeat sequence of high molecular weight subunits in order to investigate natural sequence variationsin elastomeric proteins of wheat gluten. After introduction of glutamic and aspartic acid residues, the peptidebehaved similarly to the unmodified form at low pH, but became readily water soluble at pH > 6. Substitutionof Gln for Leu at position 13 resulted in only small changes to the secondary structure of the water-insolublepeptides, as did Tyr8His and Thr11Ala. The effects of proline substitutions depended on their location: Leu13Prosubstitution had little effect on solubility and structure, but Gln6Pro substitution resulted in dramatic changes.Peptides with two Gln6Pro substitutions had similar properties to the water-insoluble parental peptide, but thosewith 6 or 10 substitutions were readily soluble. The results indicated that specific sequences influence noncovalentintermolecular interactions in wheat gluten proteins.