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1
Q34512151-64FAADE1-E71B-4B0A-B464-316E2BED9659
Q34512151-64FAADE1-E71B-4B0A-B464-316E2BED9659
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Statement
http://www.wikidata.org/entity/statement/Q34512151-64FAADE1-E71B-4B0A-B464-316E2BED9659
The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance.
P2860
Q34512151-64FAADE1-E71B-4B0A-B464-316E2BED9659
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34512151-64FAADE1-E71B-4B0A-B464-316E2BED9659
rank
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type
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wasDerivedFrom
f6dc887542fd494203654310adfb735e0d640aba
P2860
Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible