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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...

詳細記述

保存先:
書誌詳細
出版年:J Virol
主要な著者: Patton, J T, Hua, J, Mansell, E A
フォーマット: Artigo
言語:Inglês
出版事項: American Society for Microbiology (ASM) 1993
主題:
オンライン・アクセス: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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