Question

In an experiment, it was found that cys-trnacys can be converted to ala-trna cys and used in vitro system that is capable of synthesizing proteins, if the ala-trnacys where labeled with c14 in the amino acid, would the labelled ala be incorporated in the protein where ala residues are expected to occur

Answer 1

$\huge\mathfrak{Answer:}$

The GTPase activity of EF-Tu makes an important contribution to the rate and fidelity of the overall biosynthetic process. The EF-Tu•GTP complex exists for a few milliseconds, and the EF-Tu•GDP complex also exists for a similar period before it dissociates. Both of these intervals provide an opportunity for the codon-anticodon interactions to be verified (i.e., proofread). Incorrect aminoacyl-tRNAs normally dissociate during one of these periods. If the GTP analog GTPγS is used in place of GTP, hydrolysis is slowed, improving the fidelity but reducing the rate of protein synthesis. The process of protein synthesis (including the characteristics of codon-anticodon pairing already described) has clearly been optimized through evolution to balance the requirements of both speed and fidelity. Improved fidelity might diminish speed, whereas increases in speed would probably compromise fidelity.

________________

HOPE IT HELPS ❤️❤️