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Q41085989-53B08E5B-2D1A-42B7-9BAF-AB195DD5EB67
Q41085989-53B08E5B-2D1A-42B7-9BAF-AB195DD5EB67
BestRank
Statement
http://www.wikidata.org/entity/statement/Q41085989-53B08E5B-2D1A-42B7-9BAF-AB195DD5EB67
Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.
P2860
Q41085989-53B08E5B-2D1A-42B7-9BAF-AB195DD5EB67
BestRank
Statement
http://www.wikidata.org/entity/statement/Q41085989-53B08E5B-2D1A-42B7-9BAF-AB195DD5EB67
rank
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Statement
wasDerivedFrom
930dfc69108fef25de5a290414dd1a0aea82744f
P2860
The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.