NDLI: Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration

Content Provider	PubMed Central
Author	Laws, David D. Bitter, Hans-marcus L. Liu, Kai Ball, Haydn L. Kaneko, Kiyatoshi Wille, Holger Cohen, Fred E. Prusiner, Stanley B. Pines, Alexander Wemmer, David E.
Copyright Year	2001
Abstract	The secondary structure of a 55-residue fragment of the mouse prion protein, MoPrP(89–143), was studied in randomly aggregated (dried from water) and fibrillar (precipitated from water/acetonitrile) forms by 13C solid-state NMR. Recent studies have shown that the fibrillar form of the P101L mutant of MoPrP(89–143) is capable of inducing prion disease in transgenic mice, whereas unaggregated or randomly aggregated samples do not provoke disease. Through analysis of 13C chemical shifts, we have determined that both wild-type and mutant sequence MoPrP(89–143) form a mixture of β-sheet and α-helical conformations in the randomly aggregated state although the β-sheet content in MoPrP(89–143, P101L) is significantly higher than in the wild-type peptide. In a fibrillar state, MoPrP(89–143, P101L) is completely converted into β-sheet, suggesting that the formation of a specific β-sheet structure may be required for the peptide to induce disease. Studies of an analogous peptide from Syrian hamster PrP verify that sequence alterations in residues 101–117 affect the conformation of aggregated forms of the peptides.
Related Links	http://dx.doi.org/10.1073/pnas.201404298
Starting Page	11686
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	20
Volume Number	98
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2001-09-25
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.

Solid-state NMR studies of the prion protein H1 fragment

Cholesterol seco-sterol adduction inhibits the misfolding of a mutant prion protein fragment that induces neurodegeneration

Cholesterol Secosterol Adduction Inhibits the Misfolding of a Mutant Prion Protein Fragment that Induces Neurodegeneration

Solid-state NMR studies of the prion protein HI fragment

Solid-state NMR studies of the prion protein H1 fragment.

NMR structure of the bovine prion protein

Assignment and secondary structure of the YadA membrane protein by solid-state MAS NMR

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

Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration

Similar Documents

Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.

Solid-state NMR studies of the prion protein H1 fragment

Cholesterol seco-sterol adduction inhibits the misfolding of a mutant prion protein fragment that induces neurodegeneration

Cholesterol Secosterol Adduction Inhibits the Misfolding of a Mutant Prion Protein Fragment that Induces Neurodegeneration

Solid-state NMR studies of the prion protein HI fragment

Solid-state NMR studies of the prion protein H1 fragment.

NMR structure of the bovine prion protein

Assignment and secondary structure of the YadA membrane protein by solid-state MAS NMR

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

Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration