Probing enzymic transition state hydrophobicities.

Abstract

Hydrophobic interactions are important in numerous biological processes; however, the nature and extent of hydrophobic interactions in nonaqueous enzymology remain poorly defined. We have estimated the free energies of enzyme--substrate hydrophobic interactions for a model reaction catalyzed by subtilisin BPN'(from Bacillus amyloliquefaciens) in various… (More)

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@article{Wangikar1995ProbingET, title={Probing enzymic transition state hydrophobicities.}, author={Pramod P. Wangikar and J O Rich and D. S. Clark and Jonathan S. Dordick}, journal={Biochemistry}, year={1995}, volume={34 38}, pages={12302-10} }