Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-4
|
| pubmed:dateCreated |
1990-2-14
|
| pubmed:abstractText |
Five computerized methods were used to predict the secondary structure of osteopontin - a bone-derived cell attachment protein. The amino terminal one-fifth and the carboxy terminal one-third of the 301 amino acid protein contain eight alpha helices (41% of the total residues). The middle of the molecule contains a very acidic region of no predicted structure followed by two segments of beta structure which flank the cell attachment site of osteopontin. Examination of the amino acid sequence also revealed a potential calcium binding loop and two potential heparin binding sites.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0300-8207
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
21
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
15-20
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2605939-Amino Acid Sequence,
pubmed-meshheading:2605939-Animals,
pubmed-meshheading:2605939-Circular Dichroism,
pubmed-meshheading:2605939-Molecular Sequence Data,
pubmed-meshheading:2605939-Osteopontin,
pubmed-meshheading:2605939-Phosphoproteins,
pubmed-meshheading:2605939-Protein Conformation,
pubmed-meshheading:2605939-Rats,
pubmed-meshheading:2605939-Sialoglycoproteins
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Secondary structure predictions for rat osteopontin.
|
| pubmed:affiliation |
Department of Nutrition Sciences, University of Alabama, Birmingham 35294.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|