<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Rettenbacher LA</submitter><funding>H2020 Marie Skłodowska-Curie Actions</funding><pagination>268</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9773447</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>21(1)</volume><pubmed_abstract>&lt;h4>Background&lt;/h4>Escherichia coli is of central interest to biotechnological research and a widely used organism for producing proteins at both lab and industrial scales. However, many proteins remain difficult to produce efficiently in E. coli. This is particularly true for proteins that require post translational modifications such as disulfide bonds.&lt;h4>Results&lt;/h4>In this study we develop a novel approach for quantitatively investigating the ability of E. coli to produce disulfide bonds in its own proteome. We summarise the existing knowledge of the E. coli disulfide proteome and use this information to investigate the demand on this organism's quantitative oxidative folding apparatus under different growth conditions. Furthermore, we built an ordinary differential equation-based mod</pubmed_abstract><journal>Microbial cell factories</journal><pubmed_title>A quantitative interpretation of oxidative protein folding activity in Escherichia coli.</pubmed_title><pmcid>PMC9773447</pmcid><funding_grant_id>813979</funding_grant_id><pubmed_authors>Rettenbacher LA</pubmed_authors><pubmed_authors>von der Haar T</pubmed_authors></additional><is_claimable>false</is_claimable><name>A quantitative interpretation of oxidative protein folding activity in Escherichia coli.</name><description>&lt;h4>Background&lt;/h4>Escherichia coli is of central interest to biotechnological research and a widely used organism for producing proteins at both lab and industrial scales. However, many proteins remain difficult to produce efficiently in E. coli. This is particularly true for proteins that require post translational modifications such as disulfide bonds.&lt;h4>Results&lt;/h4>In this study we develop a novel approach for quantitatively investigating the ability of E. coli to produce disulfide bonds in its own proteome. We summarise the existing knowledge of the E. coli disulfide proteome and use this information to investigate the demand on this organism's quantitative oxidative folding apparatus under different growth conditions. Furthermore, we built an ordinary differential equation-based mod</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Dec</publication><modification>2026-06-22T03:17:11.633Z</modification><creation>2025-02-19T01:55:39.118Z</creation></dates><accession>S-EPMC9773447</accession><cross_references><pubmed>36550495</pubmed><doi>10.1186/s12934-022-01982-3</doi></cross_references></HashMap>