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Prodomain mutations at the subtilisin interface: correlation of binding energy and the rate of catalyzed folding.
Wang L, Ruvinov S, Strausberg S, Gallagher DT, Gilliland G, Bryan PN. Wang L, et al. Biochemistry. 1995 Nov 28;34(47):15415-20. doi: 10.1021/bi00047a004. Biochemistry. 1995. PMID: 7492541
The recent determination of the structure of a complex of the prodomain and a calcium-free subtilisin mutant has suggested how the prodomain may catalyze subtilisin folding [Bryan, P., Wang, L., Hoskins, J., Ruvinov, S., Strausberg, S., Alexander, P., Almog, O., Gil …
The recent determination of the structure of a complex of the prodomain and a calcium-free subtilisin mutant has suggested how the prodomain …
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