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Article

Folding mechanism of mutant human lysozyme C77/95A with increased secretion efficiency in yeast.

The Journal of biological chemistry - 5 Mar 1992

Taniyama Y, Ogasahara K, Yutani K, Kikuchi M

Abstract excerpt

A mutant human lysozyme C77/95A, in which Cys77 and Cys95 are replaced with alanine, has been characterized by 8-fold greater secretion in yeast (Taniyama, Y., Yamamoto, Y., Nakao, M., Kikuchi, M., and Ikehara, M. (1988) Biochem. Biophys. Res. Commun. 152, 962-967) and almost the same three-dimensional structure as wild-type human lysozyme (Inaka, K., Taniyama, Y., Kikuchi, M., Morikawa, K., and Matsushima, M....

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PMID: 1537844

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Folding mechanism of mutant human lysozyme C77/95A with increased secretion efficiency in yeast.PMID 1537844Read ↗

The crystal structure of a mutant human lysozyme C77/95A with increased secretion efficiency in yeast.Semantic proximity Read ↗

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Accelerated secretion of human lysozyme with a disulfide bond mutation.Semantic proximity Read ↗

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Evidence for difference in the roles of two cysteine residues involved in disulfide bond formation in the folding of human lysozyme.Semantic proximity Read ↗

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