| First Author | Smirnovas V | Year | 2011 |
| Journal | Nat Struct Mol Biol | Volume | 18 |
| Issue | 4 | Pages | 504-6 |
| PubMed ID | 21441913 | Mgi Jnum | J:245380 |
| Mgi Id | MGI:5919178 | Doi | 10.1038/nsmb.2035 |
| Citation | Smirnovas V, et al. (2011) Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange. Nat Struct Mol Biol 18(4):504-6 |
| abstractText | One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrP(Sc). Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrP(Sc). Our data indicate that, contrary to popular models, prion-protein conversion involves refolding of the entire region from residue ~80-90 to the C-terminus, which in PrP(Sc) consists of beta-strands and relatively short turns and/or loops, with no native alpha-helices present. |
