ANALISIS IN-SILICO PROTEIN DnaJ Bacilus stearothermophilus

Authors

  • Maureen Kumaunang Universitas Sam Ratulangi
  • Vanda S. Kamu Universitas Sam Ratulangi
  • Yohanis I. Mandik Universitas Cenderawasih

DOI:

https://doi.org/10.35799/cp.2.1.2009.63

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.

Author Biographies

  • Maureen Kumaunang, Universitas Sam Ratulangi
    Jurusan Kimia, Fakultas Matematika dan Ilmu Pengetahuan Alam,Universitas Sam Ratulangi, Manado
  • Vanda S. Kamu, Universitas Sam Ratulangi
    Jurusan Kimia, Fakultas Matematika dan Ilmu Pengetahuan Alam,Universitas Sam Ratulangi, Manado
  • Yohanis I. Mandik, Universitas Cenderawasih
    Jurusan Kimia, Fakultas Matematika dan Ilmu Pengetahuan Alam,Universitas Cenderawasih, Jayapura

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Published

2019-12-13

Issue

Vol. 2 No. 1 (2009)

Section

Articles

How to Cite

ANALISIS IN-SILICO PROTEIN DnaJ Bacilus stearothermophilus. (2019). CHEMISTRY PROGRESS, 2(1), 47-51. https://doi.org/10.35799/cp.2.1.2009.63