Article
Linear free energy relationships implicate three modes of binding for fluoroaromatic inhibitors to a mutant of carbonic anhydrase II.
Organic letters - 4 May 2000
Doyon J B, Hansen E A, Kim C Y, Chang J S, Christianson D W, Madder R D, Voet J G, Baird T A, Fierke C A, Jain A
Abstract excerpt
[figure: see text] Linear free energy relationships between binding affinity and hydrophobicity for a library of fluoroaromatic inhibitors of F131V carbonic anhydrase II (CA) implicate three modes of interaction. X-ray crystal structures suggest that F131 interacts with fluoroaromatic inhibitors, while P202, on the opposite side of the active site cleft, serves as the site of the hydrophobic contact in the case...
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