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- W2384548154 abstract "【Objective】To analyze the Chlamydiamicrovirus substructures and reveal its value in Chlamydia virus research.【Methods】The secondary structure was analyzed by the method of Gamier-Robson, Chou-Fasman and Karplus-Schulz, and its cell epitopes was analysized by the method of Kyte-Doolittle,Hopp-Woods, Emini and Jameson-Wolf. With the Proteinblast the sequences aligment were analyzed.【Results】phiCPAR39 Vp1protein has the conservative sequence. The sections of 1~10, 103~109, 158~166, 190~197, 252~260, 273~285, 310~316, 333~341, 359~367, 414~420, 466~476, 511~516 in the N-terminal of phiCPAR39 Vpl protein could be the epitopes of B cel1. Beta foldings were the priority construction to its second struction.【Conclusion】PphiCPAR39 Vpl protein has the complicated constructures.There are some antigen sites to be choozen for the recombinant rearch." @default.
- W2384548154 created "2016-06-24" @default.
- W2384548154 creator A5008408233 @default.
- W2384548154 date "2014-01-01" @default.
- W2384548154 modified "2023-09-23" @default.
- W2384548154 title "The biological polymorphism and epitope analysis of Chlamydiamicrovirus phiCPAR39 protein Vpl" @default.
- W2384548154 hasPublicationYear "2014" @default.
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