| pubmed-article:9916037 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9916037 | lifeskim:mentions | umls-concept:C0033164 | lld:lifeskim |
| pubmed-article:9916037 | lifeskim:mentions | umls-concept:C0036457 | lld:lifeskim |
| pubmed-article:9916037 | lifeskim:mentions | umls-concept:C1555029 | lld:lifeskim |
| pubmed-article:9916037 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:9916037 | lifeskim:mentions | umls-concept:C1301820 | lld:lifeskim |
| pubmed-article:9916037 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:9916037 | lifeskim:mentions | umls-concept:C1378554 | lld:lifeskim |
| pubmed-article:9916037 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9916037 | pubmed:dateCreated | 1999-3-9 | lld:pubmed |
| pubmed-article:9916037 | pubmed:abstractText | The structural transition from the cellular prion protein (PrPC) that is rich in alpha-helices to the pathological form (PrPSc) that has a high beta-sheet content seems to be the fundamental event underlying the prion diseases. Determination of the structure of PrPSc and the N-terminally truncated PrP 27-30 has been complicated by their insolubility. Here we report the solubilization of PrP 27-30 through a system of reverse micelles that yields monomeric and dimeric PrP. Although solubilization of PrP 27-30 was not accompanied by any recognizable change in secondary structure as measured by FTIR spectroscopy, it did result in a loss of prion infectivity. The formation of small two- and three-dimensional crystals upon exposure to uranyl salts argues that soluble PrP 27-30 possesses considerable tertiary structure. The crystals of PrP 27-30 grown from reverse micellar solutions suggest a novel crystallization mechanism that might be applicable for other membrane proteins. A variety of different crystal lattices diffracted up to 1.85 nm by electron microscopy. Despite the lack of measurable biological activity, the structure of PrP 27-30 in these crystals may provide insight into the structural transition that occurs during PrPSc formation. | lld:pubmed |
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| pubmed-article:9916037 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9916037 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9916037 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9916037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9916037 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9916037 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9916037 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:9916037 | pubmed:author | pubmed-author:PrusinerS BSB | lld:pubmed |
| pubmed-article:9916037 | pubmed:author | pubmed-author:WilleHH | lld:pubmed |
| pubmed-article:9916037 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9916037 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:9916037 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9916037 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9916037 | pubmed:pagination | 1048-62 | lld:pubmed |
| pubmed-article:9916037 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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