Location of intrachain disulfide bonds in the VP5* and VP8* trypsin cleavage fragments of the rhesus rotavirus spike protein VP4.

Because the rotavirus spike protein VP4 contains conserved Cys residues at positions 216, 318, 380, and 774 and, for many animal rotaviruses, also at position 203, we sought to determine whether disulfide bonds were structural elements of VP4. Electrophoretic analysis of untreated and trypsin-treate...

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Vydáno v:	J Virol
Hlavní autoři:	Patton, J T, Hua, J, Mansell, E A
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1993
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC237872/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8392619/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.67.8.4848-4855.1993
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