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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Veröffentlicht in:	J Virol
Hauptverfasser:	Patton, J T, Hua, J, Mansell, E A
Format:	Artigo
Sprache:	Inglês
Veröffentlicht:	American Society for Microbiology (ASM) 1993
Schlagworte:	Research Article
Online-Zugang:	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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