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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
2001-9-26
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pubmed:abstractText |
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 (13)C 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 (13)C chemical shifts, we have determined that both wild-type and mutant sequence MoPrP(89-143) form a mixture of beta-sheet and alpha-helical conformations in the randomly aggregated state although the beta-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 beta-sheet, suggesting that the formation of a specific beta-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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-10102274,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-10617204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-10656806,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-1438300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-6432339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-6801762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-7542350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-7703230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-7902575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-8019132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-8097911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-8105481,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-8327467,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-8464494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-8700211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-8844854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-8986833,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-9245588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-9280298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-9294167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-9391046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11562491-9811807
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
98
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11686-90
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11562491-Amino Acid Sequence,
pubmed-meshheading:11562491-Amino Acid Substitution,
pubmed-meshheading:11562491-Animals,
pubmed-meshheading:11562491-Carbon Isotopes,
pubmed-meshheading:11562491-Isotope Labeling,
pubmed-meshheading:11562491-Mice,
pubmed-meshheading:11562491-Mice, Transgenic,
pubmed-meshheading:11562491-Molecular Sequence Data,
pubmed-meshheading:11562491-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:11562491-Peptide Fragments,
pubmed-meshheading:11562491-PrPC Proteins,
pubmed-meshheading:11562491-Prion Diseases,
pubmed-meshheading:11562491-Prions,
pubmed-meshheading:11562491-Protein Conformation,
pubmed-meshheading:11562491-Protein Structure, Secondary,
pubmed-meshheading:11562491-Sequence Alignment
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pubmed:year |
2001
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pubmed:articleTitle |
Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
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pubmed:affiliation |
Department of Chemistry, University of California, Berkeley, CA 94720, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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