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Q36556932-C7E650BF-5ED7-4AB1-B339-90B00125948A
Q36556932-C7E650BF-5ED7-4AB1-B339-90B00125948A
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http://www.wikidata.org/entity/statement/Q36556932-C7E650BF-5ED7-4AB1-B339-90B00125948A
NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein.
P2860
Q36556932-C7E650BF-5ED7-4AB1-B339-90B00125948A
BestRank
Statement
http://www.wikidata.org/entity/statement/Q36556932-C7E650BF-5ED7-4AB1-B339-90B00125948A
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wasDerivedFrom
eea809a876ab39e10c6207bdcd859cdc962616ed
P2860
Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels.