Protein folding following synthesis in vitro and in vivo: Association of newly synthesized protein with 50S subunit of E. coli ribosome

Arunima Basu, Dibyendu Samanta, Arpita Bhattacharya, Anindita Das, Debasis Das, Chanchal DasGupta

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

In the accompanying paper, it was shown that a protein, while reverting to native form from the unfolded state in vitro with the help of bacterial 70S ribosome, split the latter into its subunits (50S and 30S) and remains associated with the 50S subunit. Here, we follow the fate of nascent proteins both in case of in vivo and in vitro translation system. The newly synthesised protein was found to associate with the 50S subunit in both the cases.

Original languageEnglish (US)
Pages (from-to)592-597
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume366
Issue number2
DOIs
StatePublished - Feb 8 2008
Externally publishedYes

Fingerprint

Protein folding
Protein Folding
Ribosomes
Escherichia coli
Proteins
In Vitro Techniques

Keywords

  • Association of nascent protein with 50S
  • Domain V of 23S rRNA
  • Protein folding
  • Ribosome assisted protein folding

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Protein folding following synthesis in vitro and in vivo : Association of newly synthesized protein with 50S subunit of E. coli ribosome. / Basu, Arunima; Samanta, Dibyendu; Bhattacharya, Arpita; Das, Anindita; Das, Debasis; DasGupta, Chanchal.

In: Biochemical and Biophysical Research Communications, Vol. 366, No. 2, 08.02.2008, p. 592-597.

Research output: Contribution to journalArticle

Basu, Arunima ; Samanta, Dibyendu ; Bhattacharya, Arpita ; Das, Anindita ; Das, Debasis ; DasGupta, Chanchal. / Protein folding following synthesis in vitro and in vivo : Association of newly synthesized protein with 50S subunit of E. coli ribosome. In: Biochemical and Biophysical Research Communications. 2008 ; Vol. 366, No. 2. pp. 592-597.
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