Alcohol alternative hypothesis

An alternative hypothesis is that the amino alcohol induces enantioselectivity by binding to the active site and changing its shape. An X-ray structure shows that Tris buffer (an amino alcohol) binds to the hydrophobic patch in the active site of carbonic anhydrase [58]. Similar binding of other amino alcohols could restrict the orientation of p-chlorostyrene in the active site. This second hypothesis does not explain why Femandez-Gacio et al. found no effect of buffer on enantioselectivity. 

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