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Q28361323-E7946EB5-D710-48F8-9D53-A5911D2CC548
Q28361323-E7946EB5-D710-48F8-9D53-A5911D2CC548
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http://www.wikidata.org/entity/statement/Q28361323-E7946EB5-D710-48F8-9D53-A5911D2CC548
Testing the role of chain connectivity on the stability and structure of dihydrofolate reductase from E. coli: fragment complementation and circular permutation reveal stable, alternatively folded forms
P2860
Q28361323-E7946EB5-D710-48F8-9D53-A5911D2CC548
BestRank
Statement
http://www.wikidata.org/entity/statement/Q28361323-E7946EB5-D710-48F8-9D53-A5911D2CC548
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wasDerivedFrom
7455e5cf5f0e5951eac0ae94fab547d392bfc1e1
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.