| pubmed-article:2015897 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2015897 | lifeskim:mentions | umls-concept:C0015083 | lld:lifeskim |
| pubmed-article:2015897 | lifeskim:mentions | umls-concept:C0079284 | lld:lifeskim |
| pubmed-article:2015897 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:2015897 | lifeskim:mentions | umls-concept:C2717775 | lld:lifeskim |
| pubmed-article:2015897 | lifeskim:mentions | umls-concept:C0599956 | lld:lifeskim |
| pubmed-article:2015897 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:2015897 | pubmed:dateCreated | 1991-5-21 | lld:pubmed |
| pubmed-article:2015897 | pubmed:abstractText | The solution conformation of a 21-residue vasoconstrictor peptide endothelin-1 (ET-1) in water-ethylene glycol has been determined by two-dimensional 1H-NMR spectroscopy and constrained molecular dynamics simulations. The N-terminus (residues 1-4) appears to undergo conformational averaging and no single structure consistent with the NMR constraints could be found for this region. Residues 5-8 form a turn, and residues 9-16 exist in a helical conformation. A flexible 'hinge' between residues 8-9 allows various orientations of the turn relative to the helix. Another 'hinge' at residue 17 connects the extended C-terminus to the bicyclic core region (residues 1-15). Residues important for binding and biological activity form a contiguous surface on one side of the helix, with the two disulfides extending from the other side of the helix. | lld:pubmed |
| pubmed-article:2015897 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2015897 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2015897 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2015897 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2015897 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2015897 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2015897 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2015897 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2015897 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2015897 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:2015897 | pubmed:author | pubmed-author:AndersenN HNH | lld:pubmed |
| pubmed-article:2015897 | pubmed:author | pubmed-author:ChenCC | lld:pubmed |
| pubmed-article:2015897 | pubmed:author | pubmed-author:NovotnyJJ | lld:pubmed |
| pubmed-article:2015897 | pubmed:author | pubmed-author:KrystekS... | lld:pubmed |
| pubmed-article:2015897 | pubmed:author | pubmed-author:BassolinoD... | lld:pubmed |
| pubmed-article:2015897 | pubmed:author | pubmed-author:MarschnerT... | lld:pubmed |
| pubmed-article:2015897 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2015897 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:2015897 | pubmed:volume | 281 | lld:pubmed |
| pubmed-article:2015897 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2015897 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2015897 | pubmed:pagination | 212-8 | lld:pubmed |
| pubmed-article:2015897 | pubmed:dateRevised | 2001-3-23 | lld:pubmed |
| pubmed-article:2015897 | pubmed:meshHeading | pubmed-meshheading:2015897-... | lld:pubmed |
| pubmed-article:2015897 | pubmed:meshHeading | pubmed-meshheading:2015897-... | lld:pubmed |
| pubmed-article:2015897 | pubmed:meshHeading | pubmed-meshheading:2015897-... | lld:pubmed |
| pubmed-article:2015897 | pubmed:meshHeading | pubmed-meshheading:2015897-... | lld:pubmed |
| pubmed-article:2015897 | pubmed:meshHeading | pubmed-meshheading:2015897-... | lld:pubmed |
| pubmed-article:2015897 | pubmed:meshHeading | pubmed-meshheading:2015897-... | lld:pubmed |
| pubmed-article:2015897 | pubmed:meshHeading | pubmed-meshheading:2015897-... | lld:pubmed |
| pubmed-article:2015897 | pubmed:meshHeading | pubmed-meshheading:2015897-... | lld:pubmed |
| pubmed-article:2015897 | pubmed:meshHeading | pubmed-meshheading:2015897-... | lld:pubmed |
| pubmed-article:2015897 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:2015897 | pubmed:articleTitle | Conformation of endothelin in aqueous ethylene glycol determined by 1H-NMR and molecular dynamics simulations. | lld:pubmed |
| pubmed-article:2015897 | pubmed:affiliation | Department of Macromolecular Modeling, Bristol-Myers Squibb Research Institute, Princeton, NJ 08543-4000. | lld:pubmed |
| pubmed-article:2015897 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2015897 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2015897 | lld:pubmed |
