Title : Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme.

Pub. Date : 1991 Apr 5

PMID : 2007594






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme. Disulfides lysozyme Homo sapiens
2 Our previous results using the Saccharomyces cerevisiae secretion system suggest that intramolecular exchange of disulfide bonds occurs in the folding pathway of human lysozyme in vivo (Taniyama, Y., Yamamoto, Y., Kuroki, R., and Kikuchi, M. (1990) J. Biol. Disulfides lysozyme Homo sapiens
3 These results suggest that the introduction of Cys83 and Cys91 may act to suppress the process of native disulfide bond formation through disulfide bond interchange in the folding of human lysozyme. Disulfides lysozyme Homo sapiens
4 These results suggest that the introduction of Cys83 and Cys91 may act to suppress the process of native disulfide bond formation through disulfide bond interchange in the folding of human lysozyme. Disulfides lysozyme Homo sapiens