<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ma C</submitter><funding>National Natural Science Foundation of China</funding><pagination>899578</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9085562</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13</volume><pubmed_abstract>Directed evolution is a widely-used engineering strategy for improving the stabilities or biochemical functions of proteins by repeated rounds of mutation and selection. A protein of interest is selected as the template and expressed on a molecular display platform such as a bacteriophage for engineering. Initially, the surface-displayed protein template needs to be checked against the desired target &lt;i>via&lt;/i> ELISA to examine whether the functions of the displayed template remain intact. The ELISA signal is subject to the protein-target binding affinity. A low-affinity results in a weak ELISA signal which makes it difficult to determine whether the weak signal is because of low affinity or because of poor expression of the protein. Using a methyllysine-binding chromodomain protein Cbx1 t</pubmed_abstract><journal>Frontiers in microbiology</journal><pubmed_title>Development in Detection Methods for the Expression of Surface-Displayed Proteins.</pubmed_title><pmcid>PMC9085562</pmcid><funding_grant_id>31770821</funding_grant_id><funding_grant_id>32071430</funding_grant_id><pubmed_authors>Ma C</pubmed_authors><pubmed_authors>Li S</pubmed_authors><pubmed_authors>Jiang C</pubmed_authors><pubmed_authors>Zhao D</pubmed_authors><pubmed_authors>Li R</pubmed_authors><pubmed_authors>Li L</pubmed_authors></additional><is_claimable>false</is_claimable><name>Development in Detection Methods for the Expression of Surface-Displayed Proteins.</name><description>Directed evolution is a widely-used engineering strategy for improving the stabilities or biochemical functions of proteins by repeated rounds of mutation and selection. A protein of interest is selected as the template and expressed on a molecular display platform such as a bacteriophage for engineering. Initially, the surface-displayed protein template needs to be checked against the desired target &lt;i>via&lt;/i> ELISA to examine whether the functions of the displayed template remain intact. The ELISA signal is subject to the protein-target binding affinity. A low-affinity results in a weak ELISA signal which makes it difficult to determine whether the weak signal is because of low affinity or because of poor expression of the protein. Using a methyllysine-binding chromodomain protein Cbx1 t</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022</publication><modification>2025-04-04T10:02:21.665Z</modification><creation>2025-04-04T10:02:21.665Z</creation></dates><accession>S-EPMC9085562</accession><cross_references><pubmed>35558116</pubmed><doi>10.3389/fmicb.2022.899578</doi></cross_references></HashMap>