Structural characterization of a methionine-rich, emulsifying protein from sunflower seed.
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.
Pandya
M J
MJ
Molecular Recognition Centre, School of Medical Sciences, University of Bristol, United Kingdom. maya@biols.sussex.ac.uk
Sessions
R B
RB
Williams
P B
PB
Dempsey
C E
CE
Tatham
A S
AS
Shewry
P R
PR
Clarke
A R
AR
D055516:2S Albumins, Plant; D000595:Amino Acid Sequence; D052179:Antigens, Plant; D002942:Circular Dichroism; D006368:Helianthus / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D008715:Methionine / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D012639:Seeds / Q000737:chemistry; D016415:Sequence Alignment; D014461:Ultracentrifugation
D055516:2S Albumins, Plant; D052179:Antigens, Plant; D010940:Plant Proteins; C067568:methionine-rich 2S protein, Helianthus; D008715:Methionine