Nonlinear impact of electrolyte solutions on protein dynamics

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dc.contributor.authorDaronkola, Hosein Geraili
dc.contributor.authorSöldner, Benedikt
dc.contributor.authorSingh, Himanshu
dc.contributor.authorLinser, Rasmus
dc.contributor.authorVila Verde, Ana
dc.date.accessioned2026-01-15T08:52:52Z
dc.date.available2026-01-15T08:52:52Z
dc.date.issued2024-02-23
dc.description.abstractHalophilic organisms have adapted to multi-molar salt concentrations, their cytoplasmic proteins functioning despite stronger attraction between hydrophobic groups. These proteins, of interest in biotechnology because of decreasing fresh-water resources, have excess acidic amino acids. It has been suggested that conformational fluctuations – critical for protein function – decrease in the presence of a stronger hydrophobic effect, and that an acidic proteome would counteract this decrease. However, our understanding of the salt- and acidic amino acid dependency of enzymatic activity is limited. Here, using solution NMR relaxation and molecular dynamics simulations for in total 14 proteins, we show that salt concentration has a limited and moreover non-monotonic impact on protein dynamics. The results speak against the conformational-fluctuations model, instead indicating that maintaining protein dynamics to ensure protein function is not an evolutionary driving force behind the acidic proteome of halophilic proteins.en
dc.identifier.urihttp://hdl.handle.net/2003/44679
dc.language.isoen
dc.relation.ispartofseriesChemBioChem; 25(11)
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/
dc.subjectbiological activityen
dc.subjectmolecular dynamicsen
dc.subjectprotein modelsen
dc.subjectprotein modificationsen
dc.subjectsalt effecten
dc.subject.ddc540
dc.subject.rswkBiologische Aktivität
dc.subject.rswkMolekularbewegung
dc.subject.rswkProteine
dc.subject.rswkSalzstress
dc.subject.rswkNMR-Spektroskopie
dc.subject.rswkSimulation
dc.titleNonlinear impact of electrolyte solutions on protein dynamicsen
dc.typeText
dc.type.publicationtypeResearchArticle
dcterms.accessRightsopen access
eldorado.dnb.deposittrue
eldorado.doi.registerfalse
eldorado.secondarypublicationtrue
eldorado.secondarypublication.primarycitationH. G. Daronkola, B. Söldner, H. Singh, R. Linser, A. V. Verde, ChemBioChem 2024, 25, e202400057. https://doi.org/10.1002/cbic.202400057
eldorado.secondarypublication.primaryidentifierhttps://doi.org/10.1002/cbic.202400057

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