<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Marino J</submitter><funding>Swiss National Science Foundation</funding><pagination>38-48</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4282410</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>24(1)</volume><pubmed_abstract>The interaction of the Bacillus subtilis protein Mistic with the bacterial membrane and its role in promoting the overexpression of other membrane proteins are still matters of debate. In this study, we aimed to determine whether individual helical fragments of Mistic are sufficient for its interaction with membranes in vivo and in vitro. To this end, fragments encompassing each of Mistic's helical segments and combinations of them were produced as GFP-fusions, and their cellular localization was studied in Escherichia coli. Furthermore, peptides corresponding to the four helical fragments were synthesized by solid-phase peptide synthesis, and their ability to acquire secondary structure in a variety of lipids and detergents was studied by circular dichroism spectroscopy. Both types of exp</pubmed_abstract><journal>Protein science : a publication of the Protein Society</journal><pubmed_title>Mistic's membrane association and its assistance in overexpression of a human GPCR are independent processes.</pubmed_title><pmcid>PMC4282410</pmcid><funding_grant_id>141074</funding_grant_id><pubmed_authors>Keller S</pubmed_authors><pubmed_authors>Zerbe O</pubmed_authors><pubmed_authors>Bordag N</pubmed_authors><pubmed_authors>Marino J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Mistic's membrane association and its assistance in overexpression of a human GPCR are independent processes.</name><description>The interaction of the Bacillus subtilis protein Mistic with the bacterial membrane and its role in promoting the overexpression of other membrane proteins are still matters of debate. In this study, we aimed to determine whether individual helical fragments of Mistic are sufficient for its interaction with membranes in vivo and in vitro. To this end, fragments encompassing each of Mistic's helical segments and combinations of them were produced as GFP-fusions, and their cellular localization was studied in Escherichia coli. Furthermore, peptides corresponding to the four helical fragments were synthesized by solid-phase peptide synthesis, and their ability to acquire secondary structure in a variety of lipids and detergents was studied by circular dichroism spectroscopy. Both types of exp</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015 Jan</publication><modification>2026-05-03T14:10:25.308Z</modification><creation>2019-03-27T01:42:37Z</creation></dates><accession>S-EPMC4282410</accession><cross_references><pubmed>25297828</pubmed><doi>10.1002/pro.2582</doi></cross_references></HashMap>