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dc.contributor.authorCimmperman, Piotras
dc.contributor.authorSereikaitė, Jolanta
dc.contributor.authorBumelis, Vladas Algirdas
dc.contributor.authorBaranauskienė, Lina
dc.contributor.authorBaranauskė, Simona
dc.contributor.authorJachno, Jelena
dc.contributor.authorTorresan, Jolanta
dc.contributor.authorMichailovienė, Vilma
dc.contributor.authorMatulienė, Jurgita
dc.contributor.authorMatulis, Daumantas
dc.date.accessioned2023-09-18T17:16:48Z
dc.date.available2023-09-18T17:16:48Z
dc.date.issued2008
dc.identifier.issn0006-3495
dc.identifier.other(BIS)VGT02-000017526
dc.identifier.urihttps://etalpykla.vilniustech.lt/handle/123456789/121259
dc.description.abstractEquilibrium binding ligands usually increase protein thermal stability by an amount proportional to the concentration and affinity of the ligand. High-throughput screening for the discovery of drug-like compounds uses an assay based on thermal stabilization. The mathematical description of this stabilization is well developed, and the method is widely applicable to the characterization of ligand-protein binding equilibrium. However, numerous cases have been experimentally observed where equilibrium binding ligands destabilize proteins, i.e., diminish protein melting temperature by an amount proportional to the concentration and affinity of the ligand. Here, we present a thermodynamic model that describes ligand binding to the native and unfolded (denatured) protein states explaining the combined stabilization and destabilization effects. The model also explains nonsaturation and saturation effects on the protein melting temperature when the ligand concentration significantly exceeds the protein concentration. Several examples of the applicability of the model are presented, including specific sulfonamide binding to recombinant hCAII, peptide and ANS binding to the Polo-box domain of Plk1, and zinc ion binding to the recombinant porcine growth hormone. The same ligands may stabilize and destabilize different proteins, and the same proteins may be stabilized and destabilized by different ligands.eng
dc.formatPDF
dc.format.extentp. 3222-3231
dc.format.mediumtekstas / txt
dc.language.isoeng
dc.relation.isreferencedbyScience Citation Index Expanded (Web of Science)
dc.relation.isreferencedbyBIOSIS Previews
dc.relation.isreferencedbyINSPEC
dc.relation.isreferencedbyMEDLINE
dc.relation.isreferencedbyCAB Abstracts
dc.relation.isreferencedbyCompendex
dc.relation.isreferencedbyChemical abstracts
dc.relation.isreferencedbyEmbase
dc.source.urihttps://link.springer.com/article/10.1007%2Fs10930-007-9120-1
dc.titleA quantitative model of thermal stabilization and destabilization of proteins by ligands
dc.typeStraipsnis Web of Science DB / Article in Web of Science DB
dcterms.references34
dc.type.pubtypeS1 - Straipsnis Web of Science DB / Web of Science DB article
dc.contributor.institutionBiotechnologijos institutas
dc.contributor.institutionVilniaus Gedimino technikos universitetas
dc.contributor.facultyFundamentinių mokslų fakultetas / Faculty of Fundamental Sciences
dc.contributor.departmentChemijos ir bioinžinerijos katedra / Department of Chemistry and Bioengineering
dc.subject.researchfieldT 005 - Chemijos inžinerija / Chemical engineering
dc.subject.researchfieldN 004 - Biochemija / Biochemistry
dc.subject.enCarbonic anhydrase
dc.subject.enGrowth hormone
dc.subject.enPolo-like kinase
dc.subject.enThermal denaturation
dc.subject.enThermal shift assay
dc.subject.enThermoFluor
dcterms.sourcetitleBiophysical Journal
dc.description.volumeVol. 95
dc.publisher.nameBiophysical Society
dc.publisher.cityBethesda
dc.identifier.doiLBT02-000031016
dc.identifier.doi000259393200014
dc.identifier.doi10.1007/s10930-007-9120-1
dc.identifier.elaba3839034


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