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Structural characterization of a methionine‐rich, emulsifying protein from sunflower seed
Author(s) -
Pandya Maya J.,
Sessions Richard B.,
Williams Phil B.,
Dempsey Christopher E.,
Tatham Arthur S.,
Shewry Peter R.,
Clarke Anthony R.
Publication year - 2000
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(20000215)38:3<341::aid-prot9>3.0.co;2-d
Subject(s) - sunflower , circular dichroism , chemistry , protein structure , amino acid , methionine , crystallography , biochemistry , biophysics , biology , agronomy
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. Proteins 2000;38:341–349. © 2000 Wiley‐Liss, Inc.