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Disulfide bond formation during the folding of influenza virus hemagglutinin
To study the importance of individual sulfhydryl residues during the folding and assembly in vivo of influenza virus hemagglutinin (HA), we have constructed and expressed a series of mutant HA proteins in which cysteines involved in three disulfide bonds have been substituted by serine residues. Inv...
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| Format: | Artigo |
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| Langue: | Inglês |
| Publié: |
The Rockefeller University Press
1992
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2290053/ https://ncbi.nlm.nih.gov/pubmed/1321156 |
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