<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Muzenda FL</submitter><funding>National Research Foundation</funding><funding>South African Medical Research Council</funding><pagination>27655</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12307583</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>15(1)</volume><pubmed_abstract>The main malaria parasite, Plasmodium falciparum expresses 6 Hsp70 proteins. Among them, two are Hsp110 homologues localised in the cytosol and endoplasmic reticulum. The cytosolic Hsp110 (PfHsp70-z) has been fairly studied but the ER, PfGrp170 (PfHsp70-y) has not been well characterised. PfGrp170 is essential for parasite survival and is thought to be important for protein folding during exportation of parasite proteins to the host cell cytosol. Therefore, this study optimised the conditions for its overexpression in an E. coli system and investigated the structure-functional features of Grp170 protein. The recombinant full-length version of PfGrp170 was successfully produced under native conditions. The secondary structure analysis showed a predominantly α-helical structural features whi</pubmed_abstract><journal>Scientific reports</journal><pubmed_title>Biochemical and biophysical characterization of Plasmodium falciparum glucose regulated protein 170.</pubmed_title><pmcid>PMC12307583</pmcid><funding_grant_id>148045</funding_grant_id><funding_grant_id>617193</funding_grant_id><pubmed_authors>Strauss E</pubmed_authors><pubmed_authors>Zininga T</pubmed_authors><pubmed_authors>Muzenda FL</pubmed_authors><pubmed_authors>Stofberg ML</pubmed_authors><pubmed_authors>Mthembu W</pubmed_authors></additional><is_claimable>false</is_claimable><name>Biochemical and biophysical characterization of Plasmodium falciparum glucose regulated protein 170.</name><description>The main malaria parasite, Plasmodium falciparum expresses 6 Hsp70 proteins. Among them, two are Hsp110 homologues localised in the cytosol and endoplasmic reticulum. The cytosolic Hsp110 (PfHsp70-z) has been fairly studied but the ER, PfGrp170 (PfHsp70-y) has not been well characterised. PfGrp170 is essential for parasite survival and is thought to be important for protein folding during exportation of parasite proteins to the host cell cytosol. Therefore, this study optimised the conditions for its overexpression in an E. coli system and investigated the structure-functional features of Grp170 protein. The recombinant full-length version of PfGrp170 was successfully produced under native conditions. The secondary structure analysis showed a predominantly α-helical structural features whi</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Jul</publication><modification>2026-03-16T08:59:37.994Z</modification><creation>2025-08-15T03:06:38.921Z</creation></dates><accession>S-EPMC12307583</accession><cross_references><pubmed>40730633</pubmed><doi>10.1038/s41598-025-98317-0</doi></cross_references></HashMap>