rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
2000-4-11
|
pubmed:abstractText |
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.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0887-3585
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
38
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
341-9
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:10713993-2S Albumins, Plant,
pubmed-meshheading:10713993-Amino Acid Sequence,
pubmed-meshheading:10713993-Antigens, Plant,
pubmed-meshheading:10713993-Circular Dichroism,
pubmed-meshheading:10713993-Helianthus,
pubmed-meshheading:10713993-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10713993-Mass Spectrometry,
pubmed-meshheading:10713993-Methionine,
pubmed-meshheading:10713993-Models, Molecular,
pubmed-meshheading:10713993-Molecular Sequence Data,
pubmed-meshheading:10713993-Plant Proteins,
pubmed-meshheading:10713993-Protein Structure, Quaternary,
pubmed-meshheading:10713993-Protein Structure, Secondary,
pubmed-meshheading:10713993-Seeds,
pubmed-meshheading:10713993-Sequence Alignment,
pubmed-meshheading:10713993-Ultracentrifugation
|
pubmed:year |
2000
|
pubmed:articleTitle |
Structural characterization of a methionine-rich, emulsifying protein from sunflower seed.
|
pubmed:affiliation |
Molecular Recognition Centre, School of Medical Sciences, University of Bristol, United Kingdom. maya@biols.sussex.ac.uk
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|