Show simple item record

dc.creatorAnđelković, Uroš
dc.creatorTheisgen, Stephan
dc.creatorScheidt, Holger A.
dc.creatorPetkovic, Marijana
dc.creatorHuster, Daniel
dc.creatorVujčić, Zoran
dc.date.accessioned2019-01-30T17:30:38Z
dc.date.available2019-01-30T17:30:38Z
dc.date.issued2012
dc.identifier.issn0300-9084
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/1014
dc.description.abstractUnderstanding the effect of surface charge on the stability of proteins is one prerequisite for "tailoring" proteins with increased thermal stability. Here, we investigated the origin of the altered thermal stability observed between the four recently isolated isoforms (EINV1-EINV4) of external invertase. External invertase from yeast Saccharomyces cerevisiae, a homodimeric glycoprotein, represents a widely used model for studying the influence of the glyco component on protein stability. The stability of the four isoforms of invertase decreases from EINV1 to EINV4, which is accompanied by an increase in negative surface charge density. Mass spectrometry analysis revealed that the isoforms share identical protein parts indicating that the differences in stability are the result of post-translational modifications. P-31 NMR analysis revealed that the isoforms contain negatively charged phosphate groups in diester and monoester forms attached to the glycan part. The total amount of phosphate bound to the polymannan component varies between the different isoforms. These results, together with the analysis of the amount of polymannan components, show that negative surface charge density does not entirely depend on the amount of phosphate but rather on its distribution. This suggests that charged groups bound to the glyco-component of a protein can influence the stability of glycoproteins.en
dc.publisherElsevier France-Editions Scientifiques Medicales Elsevier, Paris
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172048/RS//
dc.relationDeutscher Akademischer Austausch Dienst (DAAD)
dc.rightsrestrictedAccess
dc.sourceBiochimie
dc.subjectGlycoprotein stabilityen
dc.subjectSurface chargeen
dc.subjectPhosphorylationen
dc.subjectInvertaseen
dc.subjectIsoformen
dc.titleThe thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge densityen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractСцхеидт, Холгер A.; Хустер, Даниел; Aнђелковић, Урош; Петковиц, Маријана; Тхеисген, Степхан; Вујциц, Зоран;
dc.citation.volume94
dc.citation.issue2
dc.citation.spage510
dc.citation.epage515
dc.citation.other94(2): 510-515
dc.citation.rankM22
dc.identifier.pmid21906653
dc.identifier.doi10.1016/j.biochi.2011.08.020
dc.identifier.rcubConv_2737
dc.identifier.scopus2-s2.0-84855822854
dc.identifier.wos000300270900027
dc.type.versionpublishedVersion


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record