Supporting data on characterisation of linker switch mutants of Plasmodium falciparum heat shock protein 110 and canonical Hsp70

Simple item page
dc.contributor.authorChakafana, Grahamen_ZA
dc.contributor.authorMudau, Pertunia T.en_Za
dc.contributor.authorZininga, Tawandaen_ZA
dc.contributor.authorShonhai, Addmoreen_ZA
dc.date.accessioned2023-04-26T12:46:04Z
dc.date.available2023-04-26T12:46:04Z
dc.date.issued2021-05-29
dc.descriptionCITATION: Graham C. et al. (2021). Supporting data on characterisation of linker switch mutants of Plasmodium falciparum heat shock protein 110 and canonical Hsp70. Data in Brief 37(2021):11 pages. doi.10.1016/j.dib.2021.107177en_ZA
dc.descriptionThe original publication is available at: sciencedirect.comen_ZA
dc.description.abstractHere, we present data on characterisation of the linker of Plasmodium falciparum Hsp110 (PfHsp70-z) relative to the linker of canonical Hsp70s in support of a co-published article [1]. The linker of PfHsp70-z was switched with that of canonical Hsp70s, represented by PfHsp70–1 (cytosolic counterpart of PfHsp70-z) and E. coli Hsp70/DnaK. The datasets represent comparative analyses of PfHsp70-z, PfHsp70–1, and E. coli DnaK, relative to their linker switch mutants; PfHsp70-zLS, PfHsp70–1LS, DnaKLS, respectively. Intrinsic and extrinsic fluorescence spectroscopic analyses were employed to elucidate effects of the mutations on the structural features of the proteins. The structural conformations of the proteins were analysed in the absence as well as presence of nucleotides. In addition, stability of the proteins to stress (pH changes and urea) was also determined. Surface plasmon resonance (SPR) was employed to determine affinity of the proteins for ATP. The relative affinities of PfHsp70-z and PfHsp70–1 for the parasite cytosol localised, J domain co-chaperone, PfHsp40, was determined by SPR analysis. The effect of the linker of PfHsp70-z on the interaction of DnaKLS with DnaJ (a co-chaperone of DnaK), was similarly determined. These data could be used for future investigations involving protein-protein/ligand interactions as described in [1]. The raw data obtained using the various techniques here described are hosted in the Mendeley Data repository at [2].en_ZA
dc.description.versionPublisher’s versionen_ZA
dc.format.extent11 pages : illustrations (some color)en_ZA
dc.identifier.citationGraham C. et al. (2021). Supporting data on characterisation of linker switch mutants of Plasmodium falciparum heat shock protein 110 and canonical Hsp70. Data in Brief 37(2021):11 pages. doi.10.1016/j.dib.2021.107177en_ZA
dc.identifier.issn2352-3409 (online)en_ZA
dc.identifier.otherdoi.10.1016/j.dib.2021.107177en_ZA
dc.identifier.urihttp://hdl.handle.net/10019.1/126842
dc.language.isoen_ZAen_ZA
dc.publisherElsevier Inc.en_ZA
dc.rights.holderAuthors retain copyrighten_ZA
dc.subjectPlasmodium falciparumen_ZA
dc.subjectHeat shock proteins -- Analysisen_ZA
dc.subjectLinkeren_ZA
dc.subjectMolecular chaperones -- Mechanism of actionen_ZA
dc.subjectProteins -- Effect of stress onen_ZA
dc.subjectNucleotides -- Data processingen_ZA
dc.titleSupporting data on characterisation of linker switch mutants of Plasmodium falciparum heat shock protein 110 and canonical Hsp70en_ZA
dc.typeArticleen_ZA
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
graham_supporting_2021.pdf
Size:
736.06 KB
Format:
Adobe Portable Document Format
Description:
download article
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
1.71 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Research Articles (Biochemistry)