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Q40293155-8E5FADE7-5A0D-4280-9E7D-BB376AA5FD76
Q40293155-8E5FADE7-5A0D-4280-9E7D-BB376AA5FD76
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http://www.wikidata.org/entity/statement/Q40293155-8E5FADE7-5A0D-4280-9E7D-BB376AA5FD76
Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins.
P2860
Q40293155-8E5FADE7-5A0D-4280-9E7D-BB376AA5FD76
BestRank
Statement
http://www.wikidata.org/entity/statement/Q40293155-8E5FADE7-5A0D-4280-9E7D-BB376AA5FD76
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wasDerivedFrom
13acf7549985321dbf85be8a1d5abd925da76ba2
P2860
The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli.