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Proteins: Structure, Function, and Bioinformatics
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Research Article

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

Authors

  • Maya J. Pandya,

    Corresponding author
    1. Molecular Recognition Centre and Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol, United Kingdom
    2. IACR - Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Bristol, United Kingdom
    • Department of Biochemistry, School of Biological Sciences, University of Sussex, Falmer, East Sussex, BN1 9QG, England
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  • Richard B. Sessions,

    1. Molecular Recognition Centre and Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol, United Kingdom
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  • Phil B. Williams,

    1. Molecular Recognition Centre and Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol, United Kingdom
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  • Christopher E. Dempsey,

    1. Molecular Recognition Centre and Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol, United Kingdom
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  • Arthur S. Tatham,

    1. IACR - Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Bristol, United Kingdom
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  • Peter R. Shewry,

    1. IACR - Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Bristol, United Kingdom
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  • Anthony R. Clarke

    1. Molecular Recognition Centre and Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol, United Kingdom
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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. Proteins 2000;38:341–349. © 2000 Wiley-Liss, Inc.

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Article Information

DOI

10.1002/(SICI)1097-0134(20000215)38:3<341::AID-PROT9>3.0.CO;2-D

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Copyright © 2000 Wiley-Liss, Inc.

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Keywords

  • seed storage protein;
  • methionine-rich;
  • emulsifying agent;
  • homology model;
  • hydrophobic face

Publication History

  • Issue online:
  • Version of record online:
  • Manuscript Accepted:
  • Manuscript Received:

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