{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yano N"],"funding":["National Institute of Environmental Health Sciences","NIEHS NIH HHS"],"pagination":["756-764"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8497416"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["40(5)"],"pubmed_abstract":["Expression of recombinant proteins requires at times the aid of molecular chaperones for efficient post-translational folding into functional structure. However, predicting the compatibility of a protein substrate with the right type of chaperone to produce functional proteins is a daunting issue. To study the difference in effects of chaperones on His-tagged recombinant proteins with different characteristics, we performed in vitro proteins expression using Escherichia coli overexpressed with several chaperone 'teams': Trigger Factor (TF), GroEL/GroES and DnaK/DnaJ/GrpE, alone or in combinations, with the aim to determine whether protein secondary structure can serve as predictor for chaperone success. Protein A, which has a helix dominant structure, showed the most efficient folding with"],"journal":["The protein journal"],"pubmed_title":["Consideration on Efficient Recombinant Protein Production: Focus on Substrate Protein-Specific Compatibility Patterns of Molecular Chaperones."],"pmcid":["PMC8497416"],"funding_grant_id":["ES025379","R21 ES025379","R01 ES030227","R21 ES023936","ES023936"],"pubmed_authors":["Fedulov AV","Gregory DJ","Emi T","Yano N"],"additional_accession":[]},"is_claimable":false,"name":"Consideration on Efficient Recombinant Protein Production: Focus on Substrate Protein-Specific Compatibility Patterns of Molecular Chaperones.","description":"Expression of recombinant proteins requires at times the aid of molecular chaperones for efficient post-translational folding into functional structure. However, predicting the compatibility of a protein substrate with the right type of chaperone to produce functional proteins is a daunting issue. To study the difference in effects of chaperones on His-tagged recombinant proteins with different characteristics, we performed in vitro proteins expression using Escherichia coli overexpressed with several chaperone 'teams': Trigger Factor (TF), GroEL/GroES and DnaK/DnaJ/GrpE, alone or in combinations, with the aim to determine whether protein secondary structure can serve as predictor for chaperone success. Protein A, which has a helix dominant structure, showed the most efficient folding with","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Oct","modification":"2026-05-31T15:56:10.216Z","creation":"2025-04-04T12:46:19.47Z"},"accession":"S-EPMC8497416","cross_references":{"pubmed":["34052952"],"doi":["10.1007/s10930-021-09995-4"]}}