Effect of Glycans and the Glycophosphatidylinositol Anchor on Strain Dependent Conformations of Scrapie Prion Protein: Improved Purifications and Infrared Spectra-Reference-Cited by-同舟云学术

Effect of Glycans and the Glycophosphatidylinositol Anchor on Strain Dependent Conformations of Scrapie Prion Protein: Improved Purifications and Infrared Spectra

Published:2011-05-03 Issue:21 Volume:50 Page:4479-4490
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Baron Gerald S.¹,Hughson Andrew G.¹,Raymond Gregory J.¹,Offerdahl Danielle K.¹,Barton Kelly A.¹,Raymond Lynne D.¹,Dorward David W.¹,Caughey Byron¹

Affiliation:

1. Laboratory of Persistent Viral Diseases and ‡Microscopy Unit, Research Technology Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 59840, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi2003907

Reference60 articles.

1. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins

2. NMR characterization of the full-length recombinant murine prion protein, m PrP(23-231)

3. NMR structure of the mouse prion protein domain PrP(121–231)

4. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy

5. Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity.

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