CHEMISTRY PROGRESS
Vol 2, No 1 (2009)

ANALISIS IN-SILICO PROTEIN DnaJ Bacilus stearothermophilus

Kumaunang, Maureen (Unknown)
Kamu, Vanda S. (Unknown)
Mandik, Yohanis I. (Unknown)

Article Info

Publish Date
13 Dec 2019

Abstract

DnaJ is a chaperone which has function in facilitating folding, translocation, and degradation of protein.The aim of this research was to undertake in silico study of DnaJ protein from Bacillus stearothermophilus.Structure analysis of DnaJ B. stearothermophilus showed that it has J-domain which has two conservedmotifs, i.e. HPD and QKRA motifs. It also has cys-rich domain which has one conserved motif, i.e.CXXCXGXG. Structure prediction of DnaJ B. stearothermophilus showed that it has similar structure of Jdomainand cys-rich domain with that of DnaJ Escherichia coli.

Copyrights © 2009




Citation Download
RIS
EndNote, Reference Manager, ProCite
BibTex
Latex, Jabref
Original Source
Download Original
Google Scholar
Check in Google Scholar
Journal Info
CHEMISTRY PROGRESS
Website

Abbrev

chemprog

Publisher

Universitas Sam Ratulangi

Subject

Chemistry

Description

Majalah Ilmiah Chemistry Progress merupakan media untuk menyebarkan informasi ilmiah dan sarana komunikasi bagi para ilmuan dan cendekiawan melalui tulisan-tulisan ilmiah. Majalah Ilmiah Chemistry Progress terbit dua nomor dalam satu tahun (Mei dan November) berisi kajian penelitian dalam lingkup ...