{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ye C"],"funding":["Kentucky NASA EPSCoR","Oak Ridge Associated Universities (ORAU)","University of Kentucky"],"pagination":["239-45"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3588920"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["22(2)"],"pubmed_abstract":["Folding of outer membrane proteins (OMPs) has been studied extensively in vitro. However, most of these studies have been conducted in dilute buffer solution, which is different from the crowded environment in the cell periplasm, where the folding and membrane insertion of OMPs actually occur. Using OmpA and OmpT as model proteins and Ficoll 70 as the crowding agent, here we investigated the effect of the macromolecular crowding condition on OMP membrane insertion. We found that the presence of Ficoll 70 significantly slowed down the rate of membrane insertion of OmpA while had little effect on those of OmpT. To investigate if the soluble domain of OmpA slowed down membrane insertion in the presence of the crowding agent, we created a truncated OmpA construct that contains only the transme"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion."],"pmcid":["PMC3588920"],"funding_grant_id":["GS academic year fellowship","NNX10AV39A","Ralph E. Powe Junior Faculty Enhancement Award (Y.W.)"],"pubmed_authors":["Chai Q","Ye C","Wei Y","Zhong M"],"additional_accession":[]},"is_claimable":false,"name":"Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion.","description":"Folding of outer membrane proteins (OMPs) has been studied extensively in vitro. However, most of these studies have been conducted in dilute buffer solution, which is different from the crowded environment in the cell periplasm, where the folding and membrane insertion of OMPs actually occur. Using OmpA and OmpT as model proteins and Ficoll 70 as the crowding agent, here we investigated the effect of the macromolecular crowding condition on OMP membrane insertion. We found that the presence of Ficoll 70 significantly slowed down the rate of membrane insertion of OmpA while had little effect on those of OmpT. To investigate if the soluble domain of OmpA slowed down membrane insertion in the presence of the crowding agent, we created a truncated OmpA construct that contains only the transme","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Feb","modification":"2025-04-22T08:54:51.77Z","creation":"2019-03-27T01:05:39Z"},"accession":"S-EPMC3588920","cross_references":{"pubmed":["23225740"],"doi":["10.1002/pro.2205"]}}