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Identical RNA-protein interactions in vivo and in vitro and a scheme of folding the newly synthesized proteins by ribosomes

Das, D. (author)
Samanta, D. (author)
Hasan, S. (author)
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Das, A. (author)
Bhattacharya, A. (author)
Dasgupta, Santanu (author)
Uppsala universitet,Mikrobiologi
Chakrabarti, A. (author)
Ghorai, P. (author)
Das Gupta, C. (author)
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 (creator_code:org_t)
2012
2012
English.
In: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 287:44, s. 37508-37521
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Background: Ribosomal PTC acts as a protein folding modulator in vivo and in vitro. Results: A fixed set of nucleotides in the PTC interacts to fold polypeptides in vivo and in vitro. Conclusion: Folding all proteins through interaction with the same set of nucleotides in PTC implies they have intrinsic homology. Significance: Hundreds of proteins showed an identical cumulative hydrophobicity plot for amino acids.

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