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| Content Provider | PubMed Central |
|---|---|
| Author | Wille, H. Prusiner, S. B. |
| Abstract | 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. |
| Related Links | http://dx.doi.org/10.1016/s0006-3495(99)77270-x |
| Ending Page | 1062 |
| Page Count | 15 |
| Starting Page | 1048 |
| File Format | |
| ISSN | 00063495 |
| e-ISSN | 15420086 |
| Journal | Biophysical Journal |
| Issue Number | 2 |
| Volume Number | 76 |
| Language | English |
| Publisher Date | 1999-02-01 |
| Access Restriction | Open |
| Subject Keyword | Biophysics Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biophysics |
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