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Q30010196-FCE24E40-C9E7-435C-93CB-F691A1BE64E2
Q30010196-FCE24E40-C9E7-435C-93CB-F691A1BE64E2
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http://www.wikidata.org/entity/statement/Q30010196-FCE24E40-C9E7-435C-93CB-F691A1BE64E2
The redundancy of NMR restraints can be used to accelerate the unfolding behavior of an SH3 domain during molecular dynamics simulations
P2860
Q30010196-FCE24E40-C9E7-435C-93CB-F691A1BE64E2
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30010196-FCE24E40-C9E7-435C-93CB-F691A1BE64E2
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fee3aba13125582e1f605f113cd2533485e4f5a3
P2860
Transition states for protein folding have native topologies despite high structural variability.