Structural characterization of a methionine-rich, emulsifying protein from sunflower seed

Maya J. Pandya*, Richard B. Sessions, Phil B. Williams, Christopher E. Dempsey, Arthur S. Tatham, Peter R. Shewry, Anthony R. Clarke

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)

Abstract

The 2 S seed storage protein, sunflower albumin 8, contains an unusually high proportion of hydrophobic residues including 16 methionines in a mature protein of 103 amino acids. A structural model, based on the known structure of a related protein, has been constructed as a four-helix bundle cross- linked by four disulphide bonds. This model structure is consistent with data from circular dichroism and nuclear magnetic resonance experiments. Analysis of the model's surface shows the presence of a large hydrophobic face that may be responsible for the highly stable emulsions this protein is known to form with oil/water mixtures. (C) 2000 Wiley-Liss, Inc.

Original languageEnglish
Pages (from-to)341-349
Number of pages9
JournalProteins: Structure, Function and Genetics
Volume38
Issue number3
DOIs
Publication statusPublished - 15 Feb 2000
Externally publishedYes

Keywords

  • Emulsifying agent
  • Homology model
  • Hydrophobic face
  • Methionine-rich
  • Seed storage protein

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