| 1. |
- Chattopadhyay, S., Pal, S., Pal, D., Sarkar, D., Chandra (Sanyal), S., DasGupta, C.
(author)
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Protein folding in Escherichia coli: role of 23S ribosomal RNA
- 1999
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In: Biochim Biophys Acta. ; 1429:2, s. 293-8
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Journal article (peer-reviewed)abstract
- Post-translational control of Escherichia coli ribosome on newly synthesised polypeptide leading to its active conformation (protein folding) has been shown in the case of the enzyme beta-galactosidase. As expected, antibiotics chloramphenicol and lincomy
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| 2. |
- Pal, D., Chattopadhyay, S., Chandra (Sanyal), S., Sarkar, D., Chakraborty, A., DasGupta, C.
(author)
-
Reactivation of denatured proteins by domain V of bacterial 23S rRNA
- 1997
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In: Nucleic Acids Res. ; 25:24, s. 5047-51
-
Journal article (peer-reviewed)abstract
- In vitro transcripts containing domain V of the 23S rRNA of Escherichia coli and Bacillus subtilis can reactivate denatured proteins almost as efficiently as the total 23S rRNA. Here we show that almost the full length of domain V is required for reactiva
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| 3. |
- Pal, S., Chandra (Sanyal), S., Chowdhury, S., Sarkar, D., Ghosh, A.N., DasGupta, C.
(author)
-
Complementary role of two fragments of domain V of 23 S ribosomal RNA in protein folding
- 1999
-
In: J Biol Chem. ; 274:46, s. 32771-7
-
Journal article (peer-reviewed)abstract
- We have shown that the domain V of bacterial 23 S rRNA could fold denatured proteins to their active state. This segment of 23 S rRNA could further be split into two parts. One part containing mainly the central loop of domain V could bind denatured human
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