Construction of an 'in vitro virus' achieved a bonding efficiency of approximately 10%, yielding a population of 10^12 protein variants, which is 10^4 times that of phage display.
The in vitro virus method allows for a massive library of protein variants (10^12), significantly larger than phage display, providing a powerful tool for evolutionary molecular engineering.
Adequate means for genotype assignment to phenotype is essential in evolutionary molecular engineering. In this study, construction of 'in vitro virus' was carried out in which a genotype molecule (mRNA) covalently binds to the phenotype molecule (protein) through puromycin on the ribosome in a cell-free translation system. Bonding efficiency was approximately 10%, thus indicating a population of the in vitro virus to have approximately 10(12) protein variants, this number being 10(4) that in the phage display. The in vitro virus is useful for examining protein evolution in a test tube and the results may possibly serve as basis for a general method for selecting proteins possessing the most desirable functions.
Nemoto et al. (Mon,) reported a other. In vitro virus construction (mRNA-protein covalent binding via puromycin) vs. Phage display was evaluated on Bonding efficiency. Construction of an 'in vitro virus' achieved a bonding efficiency of approximately 10%, yielding a population of 10^12 protein variants, which is 10^4 times that of phage display.
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