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Q36393227-ACAA6DA4-C0E9-4E02-86C3-5CC16D72CE9B
Q36393227-ACAA6DA4-C0E9-4E02-86C3-5CC16D72CE9B
BestRank
Statement
http://www.wikidata.org/entity/statement/Q36393227-ACAA6DA4-C0E9-4E02-86C3-5CC16D72CE9B
Long-range side-chain-main-chain interactions play crucial roles in stabilizing the (betaalpha)8 barrel motif of the alpha subunit of tryptophan synthase.
P2860
Q36393227-ACAA6DA4-C0E9-4E02-86C3-5CC16D72CE9B
BestRank
Statement
http://www.wikidata.org/entity/statement/Q36393227-ACAA6DA4-C0E9-4E02-86C3-5CC16D72CE9B
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Statement
wasDerivedFrom
60c3921b14e4f4a8ec47325aae6281383c0f3e67
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.