| pubmed-article:9132005 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9132005 | lifeskim:mentions | umls-concept:C0033164 | lld:lifeskim |
| pubmed-article:9132005 | lifeskim:mentions | umls-concept:C0678558 | lld:lifeskim |
| pubmed-article:9132005 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:9132005 | lifeskim:mentions | umls-concept:C0205485 | lld:lifeskim |
| pubmed-article:9132005 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:9132005 | pubmed:dateCreated | 1997-4-29 | lld:pubmed |
| pubmed-article:9132005 | pubmed:abstractText | PrP(Sc) is known to be the major, if not the only, component of the infectious prion. Limited proteolysis of PrP(Sc) produces an N-terminally truncated polypeptide of about 142 residues, designated PrP 27-30. Recently, a recombinant protein (rPrP) of 142 residues corresponding to the Syrian hamster PrP 27-30 was expressed in Escherichia coli and purified (Mehlhorn et al., 1996). rPrP has been refolded into both alpha-helical and beta-sheet structures as well as various intermediates in aqueous buffers. The beta-sheet state and two pH-dependent alpha-helical states were characterized by CD and NMR. The alpha-helical conformation occurred only after the formation of an intramolecular disulfide bond, whereas the beta-sheet form was accessible either with or without the disulfide. Of the different alpha-helical forms studied, only those refolded in the pH range 5-8 were substantially soluble at physiological pH, exhibiting similar conformations and monomeric analytical sedimentation profiles throughout the above pH range. Furthermore, refolded alpha-rPrP showed NMR chemical shift dispersion typical of proteins with native conformations, although 2D NMR indicated large segments of conformational flexibility. It displayed a cooperative thermal denaturation transition; at elevated temperatures, it converted rapidly and irreversibly to the thermodynamically more stable beta-sheet form. Unfolding of alpha-rPrP by GdnHCl revealed a two-phase transition with a relatively stable folding intermediate at 2 M GdnHCl. The deltaG values were estimated to be 1.9 +/- 0.4 kcal/mol for the first phase and 6.5 +/- 1.2 kcal/mol for the second, consistent with a folding core surrounded by significant segments of flexible conformation. By NMR, alpha-rPrP(acid) isolated at pH 2 without refolding exhibited heterogeneous line widths, consistent with an acid-denatured molten globular state. We conclude that to the extent that rPrP constitutes a relevant folding domain of PrP(C), the various conformations exhibited by rPrP suggest that the PrP sequence may be intrinsically plastic in its conformations; indeed, portions of PrP(C) may possess a relatively open conformation which makes it susceptible to conversion into PrP(Sc) under appropriate conditions. | lld:pubmed |
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| pubmed-article:9132005 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9132005 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9132005 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9132005 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9132005 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9132005 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9132005 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9132005 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:9132005 | pubmed:author | pubmed-author:PrusinerS BSB | lld:pubmed |
| pubmed-article:9132005 | pubmed:author | pubmed-author:JamesT LTL | lld:pubmed |
| pubmed-article:9132005 | pubmed:author | pubmed-author:CohenF EFE | lld:pubmed |
| pubmed-article:9132005 | pubmed:author | pubmed-author:GrothDD | lld:pubmed |
| pubmed-article:9132005 | pubmed:author | pubmed-author:MehlhornII | lld:pubmed |
| pubmed-article:9132005 | pubmed:author | pubmed-author:ZhangHH | lld:pubmed |
| pubmed-article:9132005 | pubmed:author | pubmed-author:BaldwinM AMA | lld:pubmed |
| pubmed-article:9132005 | pubmed:author | pubmed-author:StockelJJ | lld:pubmed |
| pubmed-article:9132005 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9132005 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:9132005 | pubmed:volume | 36 | lld:pubmed |
| pubmed-article:9132005 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9132005 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9132005 | pubmed:pagination | 3543-53 | lld:pubmed |
| pubmed-article:9132005 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9132005 | pubmed:meshHeading | pubmed-meshheading:9132005-... | lld:pubmed |
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| pubmed-article:9132005 | pubmed:meshHeading | pubmed-meshheading:9132005-... | lld:pubmed |
| pubmed-article:9132005 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9132005 | pubmed:articleTitle | Physical studies of conformational plasticity in a recombinant prion protein. | lld:pubmed |
| pubmed-article:9132005 | pubmed:affiliation | Department of Neurology, University of California, San Francisco 94143, USA. | lld:pubmed |
| pubmed-article:9132005 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9132005 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9132005 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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