AI Article Synopsis
- The study focuses on developing a method for correlating genotype (mRNA) with phenotype (protein) using an 'in vitro virus' system.
- The bonding efficiency of the genotype to phenotype was around 10%, leading to the creation of roughly 10^12 protein variants, significantly higher than traditional methods like phage display.
- This in vitro virus technique allows for the investigation of protein evolution in a controlled environment, potentially aiding in the selection of proteins with desirable functions in future research.
Article Abstract
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.
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| http://dx.doi.org/10.1016/s0014-5793(97)01026-0 | DOI Listing |
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