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1
Q43029878-3283F2AB-202A-4D3B-8345-033F169E5ABD
Q43029878-3283F2AB-202A-4D3B-8345-033F169E5ABD
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http://www.wikidata.org/entity/statement/Q43029878-3283F2AB-202A-4D3B-8345-033F169E5ABD
Slow-tight binding inhibition of xylanase by an aspartic protease inhibitor: kinetic parameters and conformational changes that determine the affinity and selectivity of the bifunctional nature of the inhibitor.
P2860
Q43029878-3283F2AB-202A-4D3B-8345-033F169E5ABD
BestRank
Statement
http://www.wikidata.org/entity/statement/Q43029878-3283F2AB-202A-4D3B-8345-033F169E5ABD
rank
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type
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wasDerivedFrom
465e8da8daf5477982448aae0778e2d8c119734f
P2860
Crystal structure at 1.8 A resolution and proposed amino acid sequence of a thermostable xylanase from Thermoascus aurantiacus