| pubmed-article:17078073 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17078073 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:17078073 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:17078073 | lifeskim:mentions | umls-concept:C1869236 | lld:lifeskim |
| pubmed-article:17078073 | lifeskim:mentions | umls-concept:C0121463 | lld:lifeskim |
| pubmed-article:17078073 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:17078073 | pubmed:dateCreated | 2006-12-13 | lld:pubmed |
| pubmed-article:17078073 | pubmed:abstractText | Electron microscopy and infrared and Raman spectroscopy have been used here to study the morphology, size distribution, secondary and tertiary structures of protein particles assembled from a truncated hepatitis C virus (HCV) core protein covering the first 120 aa. Particles of pure protein, having similar morphology and size distribution of those of nucleocapsids found in sera from HCV-infected patients, have been visualized for the first time. The secondary structure of these protein particles involve beta-sheet enrichment in relation to its protein monomer. Tertiary/quaternary structure has also been studied using the dynamics of H/D exchange. With this aim infrared spectra were measured as a function of H/D exchange time and subsequently analyzed by principal component analysis and two-dimensional correlation spectroscopy. Temporal dynamics of exchange for these protein particles were as follows: arginine residues exchanged first, followed by turn and unordered structures, followed by beta-sheets which may act as linkers of protein monomers. | lld:pubmed |
| pubmed-article:17078073 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17078073 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17078073 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17078073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17078073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17078073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17078073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17078073 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17078073 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:17078073 | pubmed:issn | 1097-0134 | lld:pubmed |
| pubmed-article:17078073 | pubmed:author | pubmed-author:NamestnickJJ | lld:pubmed |
| pubmed-article:17078073 | pubmed:author | pubmed-author:MolinaMarinaM | lld:pubmed |
| pubmed-article:17078073 | pubmed:author | pubmed-author:Rodríguez-Cas... | lld:pubmed |
| pubmed-article:17078073 | pubmed:copyrightInfo | (c) 2006 Wiley-Liss, Inc. | lld:pubmed |
| pubmed-article:17078073 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17078073 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17078073 | pubmed:volume | 66 | lld:pubmed |
| pubmed-article:17078073 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17078073 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17078073 | pubmed:pagination | 110-7 | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:meshHeading | pubmed-meshheading:17078073... | lld:pubmed |
| pubmed-article:17078073 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17078073 | pubmed:articleTitle | Spectroscopic study of conformational changes accompanying self-assembly of HCV core protein. | lld:pubmed |
| pubmed-article:17078073 | pubmed:affiliation | Instituto de Estructura de la Materia (CSIC), Serrano 121, 28006 Madrid, Spain. | lld:pubmed |
| pubmed-article:17078073 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17078073 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:951475 | entrezgene:pubmed | pubmed-article:17078073 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17078073 | lld:entrezgene |
