| pubmed-article:8507644 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8507644 | lifeskim:mentions | umls-concept:C0023820 | lld:lifeskim |
| pubmed-article:8507644 | lifeskim:mentions | umls-concept:C0162807 | lld:lifeskim |
| pubmed-article:8507644 | lifeskim:mentions | umls-concept:C0205666 | lld:lifeskim |
| pubmed-article:8507644 | lifeskim:mentions | umls-concept:C0332161 | lld:lifeskim |
| pubmed-article:8507644 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8507644 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8507644 | lifeskim:mentions | umls-concept:C0439810 | lld:lifeskim |
| pubmed-article:8507644 | lifeskim:mentions | umls-concept:C0260249 | lld:lifeskim |
| pubmed-article:8507644 | lifeskim:mentions | umls-concept:C0597177 | lld:lifeskim |
| pubmed-article:8507644 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8507644 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8507644 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:8507644 | pubmed:dateCreated | 1993-7-9 | lld:pubmed |
| pubmed-article:8507644 | pubmed:abstractText | The secondary structure of the human low-density lipoprotein (LDL) apo B-100 fragment embedded in the lipid domain of the particle has been investigated by Fourier transform attenuated total reflection infrared spectroscopy (FTIR-ATR). The solvent-exposed region of the protein was hydrolyzed by using different proteases (alpha-chymotrypsin, trypsin, proteinase K) for incubation times varying between 24 min and 48 h. Analysis of the FTIR-ATR spectra after repurification of the digested LDL particle indicates the same trend for all the hydrolysis conditions tested: the peptides remaining associated with the particle are rich in beta-sheet structure. Dichroism spectra reveal that at least part of the beta-sheets is associated with the phospholipid component of the particle. | lld:pubmed |
| pubmed-article:8507644 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8507644 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8507644 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8507644 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8507644 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8507644 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8507644 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8507644 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8507644 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8507644 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8507644 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8507644 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8507644 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:8507644 | pubmed:author | pubmed-author:RuysschaertJ... | lld:pubmed |
| pubmed-article:8507644 | pubmed:author | pubmed-author:RosseneuMM | lld:pubmed |
| pubmed-article:8507644 | pubmed:author | pubmed-author:GoormaghtighE... | lld:pubmed |
| pubmed-article:8507644 | pubmed:author | pubmed-author:CabiauxVV | lld:pubmed |
| pubmed-article:8507644 | pubmed:author | pubmed-author:De MeutterJJ | lld:pubmed |
| pubmed-article:8507644 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8507644 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8507644 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:8507644 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8507644 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8507644 | pubmed:pagination | 6104-10 | lld:pubmed |
| pubmed-article:8507644 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8507644 | pubmed:meshHeading | pubmed-meshheading:8507644-... | lld:pubmed |
| pubmed-article:8507644 | pubmed:meshHeading | pubmed-meshheading:8507644-... | lld:pubmed |
| pubmed-article:8507644 | pubmed:meshHeading | pubmed-meshheading:8507644-... | lld:pubmed |
| pubmed-article:8507644 | pubmed:meshHeading | pubmed-meshheading:8507644-... | lld:pubmed |
| pubmed-article:8507644 | pubmed:meshHeading | pubmed-meshheading:8507644-... | lld:pubmed |
| pubmed-article:8507644 | pubmed:meshHeading | pubmed-meshheading:8507644-... | lld:pubmed |
| pubmed-article:8507644 | pubmed:meshHeading | pubmed-meshheading:8507644-... | lld:pubmed |
| pubmed-article:8507644 | pubmed:meshHeading | pubmed-meshheading:8507644-... | lld:pubmed |
| pubmed-article:8507644 | pubmed:meshHeading | pubmed-meshheading:8507644-... | lld:pubmed |
| pubmed-article:8507644 | pubmed:meshHeading | pubmed-meshheading:8507644-... | lld:pubmed |
| pubmed-article:8507644 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8507644 | pubmed:articleTitle | Secondary structure of the particle associating domain of apolipoprotein B-100 in low-density lipoprotein by attenuated total reflection infrared spectroscopy. | lld:pubmed |
| pubmed-article:8507644 | pubmed:affiliation | Laboratoire de Chimie Physique des Macromolécules aux Interfaces, Université Libre de Bruxelles, Belgium. | lld:pubmed |
| pubmed-article:8507644 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8507644 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8507644 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8507644 | lld:pubmed |
