| pubmed-article:1063402 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1063402 | lifeskim:mentions | umls-concept:C0037659 | lld:lifeskim |
| pubmed-article:1063402 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:1063402 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:1063402 | lifeskim:mentions | umls-concept:C0012222 | lld:lifeskim |
| pubmed-article:1063402 | lifeskim:mentions | umls-concept:C0597429 | lld:lifeskim |
| pubmed-article:1063402 | lifeskim:mentions | umls-concept:C0008813 | lld:lifeskim |
| pubmed-article:1063402 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:1063402 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:1063402 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:1063402 | pubmed:dateCreated | 1976-7-6 | lld:pubmed |
| pubmed-article:1063402 | pubmed:abstractText | Somatostatin is a hypothalamic tetradeca peptide that inhibits the release of growth hormone insulin, and glucagon. The circular dichroism spectrum is characterized by negative extrema at 238 nm and 270 nm, and a positive extremum at 225 nm. The far ultraviolet circular dichroism spectrum is consistent with the presence of ordered secondary structure such as beta-structure, but not alpha-helix. Sedimentation equilibrium results demonstrate that somatostatin exists in its monomeric form (i.e., a molecular weight of 1610 +/- 36 was obtained) and, thus, the structure must arise from intramolecular interactions. The diffusion constant of somatostatin was estimated to be 1.66 X 10(-6) cm2/sec. These data are consistent with an ellipsoidal rather than a spherical shape. The magnitude of the ellipticity at both 225 nm and 238 nm is quite dependent on guanidinium hydrochloride concentration; the midpoint occurs at about 3 M and the transition is cooperative-like. These data strongly suggest that somatostatin has a stable conformation in aqueous solution. A model, consistent with the results of the physicochemical studies and with semi-empirical rules for secondary structure formation, is proposed for somatostatin. The proposed structure consists of a hairpin loop with several residues in an antiparallel beta-pleated sheet, is somewhat elongated, and contains a hydrophobic domain at one end and a hydrophilic domain at the other end. | lld:pubmed |
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| pubmed-article:1063402 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1063402 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1063402 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1063402 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:1063402 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1063402 | pubmed:author | pubmed-author:PuettDD | lld:pubmed |
| pubmed-article:1063402 | pubmed:author | pubmed-author:HolladayL ALA | lld:pubmed |
| pubmed-article:1063402 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1063402 | pubmed:volume | 73 | lld:pubmed |
| pubmed-article:1063402 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1063402 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1063402 | pubmed:pagination | 1199-202 | lld:pubmed |
| pubmed-article:1063402 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1063402 | pubmed:meshHeading | pubmed-meshheading:1063402-... | lld:pubmed |
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| pubmed-article:1063402 | pubmed:meshHeading | pubmed-meshheading:1063402-... | lld:pubmed |
| pubmed-article:1063402 | pubmed:meshHeading | pubmed-meshheading:1063402-... | lld:pubmed |
| pubmed-article:1063402 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:1063402 | pubmed:articleTitle | Somatostatin conformation: evidence for a stable intramolecular structure from circular dichroism, diffusion, and sedimentation equilibrium. | lld:pubmed |
| pubmed-article:1063402 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1063402 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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