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CS716 PAST PAPERS

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CS201 FINAL TERM SOLVED PAPERS BY WAQAR SIDHU.ENG101 FINAL TERM SOLVED MCQS.CS403 CURRENT FINAL TERM PAPERS.CS101 FINAL TERM SOLVED PAPERS BY MOAAZ MEGA FILE. CS201 FINAL TERM SOLVED PAPERS BY MOAAZ MEGA FILE. CS205 FINAL TERM PAST PAPERS. CS204 FINAL TERM PAST PAPERS. CS301 FINAL TERM SOLVED PAPERS BY MOAAZ. CS304 FINAL TERM SOLVED PAPERS BY MOAAZ. CS311 FINAL TERM SOLVED PAPERS BY MOAAZ. CS401 FINAL TERM SOLVED PAPERS BY MOAAZ

 

Another methionine charge. second dRNA, now
Taking a dipite, it is transferred to the B site as a ribosome
5-to-3 with codon mRNA. direction going.
The stretching process continues, and the polypeptide
The chain grows as the steps are repeated:

Next the charged DNA enters the open A site.
Its amino acids form peptide bonds with amino acids
series at the base of P, so it increases
Polypeptide chain from dRNA to site B.
An on-site team (-COOH).

How does a larger ribosomal subunit change this binding? In 1992, at the University of California at Santa Cruz, Harry Knowler and his colleagues removed all proteins in a large subset.
Catalytic peptide bond formation. But if the rRNA is destroyed, the transfer function in the peptide will also be destroyed. in part.

rRNA eventually communicates in large subsets
The amino acid is charged by the attached DNA. Like this
rRNA appears to be the catalyst. This situation is very unusual because proteins are usually biological catalysts.
Systems Recent purification and crystallization of ribosomes has allowed scientists to study their structure
Description and catalytic role of rRNA in peptidal transfer
Function confirmed.

The stretch continues and the polypeptide grows
After the first dRNA released its methionine, it retracted
From the ribosome, return to the cytosol

 

 

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