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Structural characterization of a methionine-rich, emulsifying protein from sunflower seed
M J Pandya1, R B Sessions, P B Williams
1Molecular Recognition Centre, School of Medical Sciences, University of Bristol, United Kingdom. maya@biols.sussex.ac.uk
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.