Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Chanchal DasGupta"'
Autor:
Chanchal Dasgupta
Publikováno v:
ASME 2019 India Oil and Gas Pipeline Conference.
Polyethylene pipes and Steel pipes with 3LPE coatings are integral part of a citygas distribution network. These are being used in India since late 80’s. Standard MDPE and HDPE materials are Butene copolymers of Ethylene, where Butene (C4) is added
Autor:
Debasis Das, Dibyendu Samanta, Arpita Bhattacharya, Anindita Das, Arunima Basu, Chanchal DasGupta
Publikováno v:
Biochemical and Biophysical Research Communications. 384:137-140
The peptidyl transferase center (PTC), present in the domain V of 23S rRNA of bacteria can act as a general protein folding modulator. Any general function of a nucleic acid polymer (DNA or RNA) is always related to specific sequence/sequences. The r
Autor:
Debasis Das, Chanchal DasGupta, Anindita Das, Jaydip Ghosh, Dibyendu Samanta, Debashis Mukhopadhyay, Saheli Chowdhury, Arunima Basu, Saumen Pal, Arpita Bhattacharya
Publikováno v:
Journal of Bacteriology. 190:3344-3352
The peptidyl transferase center, present in domain V of 23S rRNA of eubacteria and large rRNA of plants and animals, can act as a general protein folding modulator. Here we show that a few specific nucleotides in Escherichia coli domain V RNA bind to
Autor:
Arpita Bhattacharya, Anindita Das, Dibyendu Samanta, Chanchal DasGupta, Debasis Das, Arunima Basu
Publikováno v:
Biochemical and Biophysical Research Communications. 366:592-597
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 subu
Autor:
Arunima Basu, Arpita Bhattacharya, Chanchal DasGupta, Saheli Chowdhury, Dibyendu Samanta, Debasis Das, Anindita Das, Jaydip Ghosh
Publikováno v:
Biochemical and Biophysical Research Communications. 366:598-603
Folding of unfolded protein on Escherichia coli 70S ribosome is accompanied by rapid dissociation of the ribosome into 50S and 30S subunits. The dissociation rate of 70S ribosome with unfolded protein is much faster than that caused by combined effec
Autor:
Chanchal DasGupta, Arunima Basu, Dhruba K. Chattoraj, Arpita Bhattacharya, Debashis Pal, Saumen Pal, Jaydip Ghosh, Saheli Chowdhuri
Publikováno v:
Molecular Microbiology. 48:1679-1692
Bacterial ribosomes or their 50S subunit can refold many unfolded proteins. The folding activity resides in domain V of 23S RNA of the 50S subunit. Here we show that ribosomes can also refold a denatured chaperone, DnaK, in vitro, and the activity ma
Autor:
Suparna Chandra, Sanyal, Saumen, Pal, Saheli, Chowdhury, Chanchal, DasGupta, Saheli, Chaudhuri
Publikováno v:
Nucleic Acids Research. 30:2390-2397
The role of the 50S particle of Escherichia coli ribosome and its 23S rRNA in the refolding and subunit association of dimeric porcine heart cytoplasmic malate dehydrogenase (s-MDH) has been investigated. The self-reconstitution of s-MDH is governed
Autor:
Chanchal DasGupta, Dibyendu Sarkar
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1296:85-94
GdnHCl-induced unfolding and reversible folding of beta-lactamase from E. coli have been investigated by measuring enzymatic activity, fluorescence emission and far-UV circular dichroism as indices of the extent of denaturation. The non-coincidence o
Publikováno v:
Biochemical Journal. 300:717-721
Escherichia coli ribosomes were used to refold denatured lactate dehydrogenase from porcine muscle. This activity of ribosomes, unlike most of the chaperons, did not require the presence of ATP. The molar concentration of ribosomes required for this
Autor:
Jaydip, Ghosh, Arunima, Basu, Saumen, Pal, Saheli, Chowdhuri, Arpita, Bhattacharya, Debashis, Pal, Dhruba K, Chattoraj, Chanchal, DasGupta
Publikováno v:
Molecular microbiology. 48(6)
Bacterial ribosomes or their 50S subunit can refold many unfolded proteins. The folding activity resides in domain V of 23S RNA of the 50S subunit. Here we show that ribosomes can also refold a denatured chaperone, DnaK, in vitro, and the activity ma