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. 1998 Sep 15;95(19):11030-1.

doi: 10.1073/pnas.95.19.11030.

Prions

D Westaway¹, G Telling, S Priola

Affiliations

Affiliation

¹ University of Toronto, Centre for Research in Neurodegenerative Diseases, Tanz Neuroscience Building, 6 Queen's Park Crescent West, Toronto, Ontario, M5S 3H2, Canada.

PMID: 9736680
PMCID: PMC33890
DOI: 10.1073/pnas.95.19.11030

Prions

D Westaway et al. Proc Natl Acad Sci U S A. 1998.

. 1998 Sep 15;95(19):11030-1.

doi: 10.1073/pnas.95.19.11030.

Authors

D Westaway¹, G Telling, S Priola

Affiliation

¹ University of Toronto, Centre for Research in Neurodegenerative Diseases, Tanz Neuroscience Building, 6 Queen's Park Crescent West, Toronto, Ontario, M5S 3H2, Canada.

PMID: 9736680
PMCID: PMC33890
DOI: 10.1073/pnas.95.19.11030

No abstract available

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Figures

Figure 1
Schematic diagram showing the flexibility of the polypeptide chain for PrP(29-231). The structure of the portion of the protein representing residues 90–231 was taken from the coordinates of PrP(90-231) (17). The remainder of the sequence was hand-built for illustration purposes only. The color scale shows the heteronuclear [¹H]-¹⁵N NOE data, from red for the lowest (most negative) values, where the polypepide is most flexible, to blue for the highest (most positive) values in the most structured and rigid regions of the protein. (Courtesy of the University of California, San Francisco and reproduced with permission from ref. .)

See this image and copyright information in PMC

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