Structural characterization of a methionine-rich, emulsifying protein from sunflower seed
✍ Scribed by Maya J. Pandya; Richard B. Sessions; Phil B. Williams; Christopher E. Dempsey; Arthur S. Tatham; Peter R. Shewry; Anthony R. Clarke
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 414 KB
- Volume
- 38
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
✦ Synopsis
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.