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ANALISIS IN-SILICO PROTEIN TIOL-DISULFIDA ISOMERASE Bacillus sp . RP1 ABSTRAK Pelipatan protein membutuhkan bantuan molekul chaperone serta katalis pelipatan. Penelitian ini bertujuan untuk mengkarakterisasi produk gen tiol-disulfida oksidoreduktase dari sumber organisme termofilik Bacillus sp. RP1. Metode yang dilaksanakan untuk mencapai tujuan tersebut, adalah mengkarakterisasi produk gen yang dihasilkan dengan menggunakan analisis in-silico. Dari hasil penelitian diperoleh bahwa karakterisasi terhadap produk gen yang dihasilkan menunjukkan adanya tiga protein, yaitu Bdbdred, Bdbdox, dan Etda, yang memiliki motif tioredoksin dan DsbA, serta sisi aktif dan sisi pengikatan dengan atom Zn. Prediksi struktur ketiga protein tersebut menunjukkan kemiripan satu sama lain. Kata kunci : Bdbd, chaperone, DsbA, tiol-disulfida oksidoreduktase, tioredoksin ANALYSIS OF IN-SILICO TIOL DISULFIDE ISOMERASE PROTEIN Bacillus sp . RP1 ABSTRACT Protein folding is facilitated by chaperone molecule as well as folding catalysts. The aim of this research was to characterize the gene product of thiol-disulfide oxidoreductase gene from thermophylic organism Bacillus sp. RP1, by using in-silico analysis. The characteristic of the gene product indicated three proteins, i.e. Bdbdred, Bdbdox, and Etda, which have thioredoxin motif, DsbA motif, active site and bonding site with Zn. The structure predicted of these three proteins showed similarity among them. Keywords : Bdbd, chaperone, DsbA, thiol-disulfide oxidoreductase, thioredoxin

Analisis In-Silico Protein Tiol-Disulfida Isomerase Bacillus sp. RP1