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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1989-8-8
|
| pubmed:abstractText |
The conformation flexibility of the tetradecapeptide hormone bombesin and its synthetic antagonist (DPhe12, Leu14)-bombesin has been studied using nuclear magnetic resonance and circular dichroism techniques. The spectral features observed indicate that the ordered structure present in the C-terminal pentapeptide moiety of native BBS is lost in the (DPhe12, Leu14) analog.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0006-291X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
30
|
| pubmed:volume |
161
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
987-93
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2545203-Bombesin,
pubmed-meshheading:2545203-Circular Dichroism,
pubmed-meshheading:2545203-Magnetic Resonance Spectroscopy,
pubmed-meshheading:2545203-Protein Conformation,
pubmed-meshheading:2545203-Receptors, Bombesin,
pubmed-meshheading:2545203-Receptors, Neurotransmitter,
pubmed-meshheading:2545203-Structure-Activity Relationship
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Conformation studies on bombesin receptor antagonists: 500 MHz NMR and CD characterization of synthetic (D-Phe12, Leu14)-bombesin.
|
| pubmed:affiliation |
Institute of Industrial Chemistry, University of Padova, Italy.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|