| pubmed-article:12051766 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12051766 | lifeskim:mentions | umls-concept:C0600115 | lld:lifeskim |
| pubmed-article:12051766 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:12051766 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:12051766 | pubmed:dateCreated | 2002-6-7 | lld:pubmed |
| pubmed-article:12051766 | pubmed:abstractText | Conformational features of the C-terminal carboxyamidated pentadecapeptide of CCK (S(19)HRISDRD[SO(4)]-YMGWMDF(33)-NH(2)) were determined by NMR spectroscopy in a zwitterionic membrane-mimetic solvent system, composed of DPC micelles. The C-terminal octapeptide consisted of a well-defined pseudohelix that was nearly identical to the structure previously reported for nonsulfated CCK-8 in the same solvent system. N-terminal amino acids of CCK-15 were highly disordered, with no clear conformational preference. Extensive NOE-restrained molecular dynamics simulations of the CCK-15/CCK(1)-R complex suggested that almost all the experimentally determined intermolecular contact points provided by NMR, site-directed mutagenesis, and photoaffinity labeling could be simultaneously satisfied, when the N-terminus of the ligand is placed in close spatial proximity to the N-terminus of the receptor. | lld:pubmed |
| pubmed-article:12051766 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12051766 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12051766 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12051766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12051766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12051766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12051766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12051766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12051766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12051766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12051766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12051766 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12051766 | pubmed:month | May | lld:pubmed |
| pubmed-article:12051766 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:12051766 | pubmed:author | pubmed-author:MoroderLuisL | lld:pubmed |
| pubmed-article:12051766 | pubmed:author | pubmed-author:MierkeDale... | lld:pubmed |
| pubmed-article:12051766 | pubmed:author | pubmed-author:GiragossianCr... | lld:pubmed |
| pubmed-article:12051766 | pubmed:author | pubmed-author:StoneShaneS | lld:pubmed |
| pubmed-article:12051766 | pubmed:author | pubmed-author:PapiniAnna... | lld:pubmed |
| pubmed-article:12051766 | pubmed:copyrightInfo | (c) 2002 Elsevier Science (USA). | lld:pubmed |
| pubmed-article:12051766 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12051766 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:12051766 | pubmed:volume | 293 | lld:pubmed |
| pubmed-article:12051766 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12051766 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12051766 | pubmed:pagination | 1053-9 | lld:pubmed |
| pubmed-article:12051766 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12051766 | pubmed:meshHeading | pubmed-meshheading:12051766... | lld:pubmed |
| pubmed-article:12051766 | pubmed:meshHeading | pubmed-meshheading:12051766... | lld:pubmed |
| pubmed-article:12051766 | pubmed:meshHeading | pubmed-meshheading:12051766... | lld:pubmed |
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| pubmed-article:12051766 | pubmed:meshHeading | pubmed-meshheading:12051766... | lld:pubmed |
| pubmed-article:12051766 | pubmed:meshHeading | pubmed-meshheading:12051766... | lld:pubmed |
| pubmed-article:12051766 | pubmed:meshHeading | pubmed-meshheading:12051766... | lld:pubmed |
| pubmed-article:12051766 | pubmed:meshHeading | pubmed-meshheading:12051766... | lld:pubmed |
| pubmed-article:12051766 | pubmed:meshHeading | pubmed-meshheading:12051766... | lld:pubmed |
| pubmed-article:12051766 | pubmed:meshHeading | pubmed-meshheading:12051766... | lld:pubmed |
| pubmed-article:12051766 | pubmed:meshHeading | pubmed-meshheading:12051766... | lld:pubmed |
| pubmed-article:12051766 | pubmed:meshHeading | pubmed-meshheading:12051766... | lld:pubmed |
| pubmed-article:12051766 | pubmed:meshHeading | pubmed-meshheading:12051766... | lld:pubmed |
| pubmed-article:12051766 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12051766 | pubmed:articleTitle | Conformational and molecular modeling studies of sulfated cholecystokinin-15. | lld:pubmed |
| pubmed-article:12051766 | pubmed:affiliation | Department of Chemistry, Division of Biology & Medicine, Brown University, Providence, RI 02912, USA. | lld:pubmed |
| pubmed-article:12051766 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12051766 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
