0000000001308070

AUTHOR

Riikka Ihalin

showing 4 related works from this author

Decreased temperature increases the expression of a disordered bacterial late embryogenesis abundant (LEA) protein that enhances natural transformati…

2021

Late embryogenesis abundant (LEA) proteins are important players in the management of responses to stressful conditions, such as drought, high salinity, and changes in temperature. Many LEA proteins do not have defined three-dimensional structures, so they are intrinsically disordered proteins (IDPs) and are often highly hydrophilic. Although LEA-like sequences have been identified in bacterial genomes, the functions of bacterial LEA proteins have been studied only recently. Sequence analysis of outer membrane interleukin receptor I (BilRI) from the oral pathogen Aggregatibacter actinomycetemcomitans indicated that it shared sequence similarity with group 3/3b/4 LEA proteins. Comprehensive …

Cold shock proteinEmbryonic DevelopmentInfectious and parasitic diseasesRC109-216Aggregatibacter actinomycetemcomitansbakteeritkylmänkestävyysNMR spectroscopyBacterial Proteinsnmr spectroscopyDNA transformation competencelate embryogenesis abundant proteinHumansNMR-spektroskopiaPlant Proteinsaggregatibacter actinomycetemcomitanscold shock proteinlate embryogenesisBiochemistry and Molecular BiologyTemperatureIntrinsically Disordered Proteinsabundant proteindna transformation competencelämpötilaproteiinitBiokemi och molekylärbiologiResearch ArticleResearch PaperVirulence
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Dispersion from Cα or NH: 4D experiments for backbone resonance assignment of intrinsically disordered proteins

2020

AbstractResonance assignment of intrinsically disordered proteins is remarkably challenging due to scant chemical shift dispersion arising from conformational heterogeneity. The challenge is even greater if repeating segments are present in the amino acid sequence. To forward unambiguous resonance assignment of intrinsically disordered proteins, we present iHACANCO, HACACON and (HACA)CONCAHA, three Hα-detected 4D experiments with Cα as an additional dimension. In addition, we present (HACA)CON(CA)NH and (HACA)N(CA)CONH, new 4D Hα-start, HN-detect experiments which have two NH dimensions to enhance peak dispersion in a sequential walk through C′, NH and HN, and provide more accurate NH/HN ch…

0303 health sciencesChemical substanceChemistryChemical shiftIDPintrinsically disordered proteinresonanssi010402 general chemistryIntrinsically disordered proteinsAggregatibacter actinomycetemcomitans01 natural sciencesBiochemistryResonance (particle physics)bakteerit0104 chemical sciences03 medical and health sciencesCrystallographyBilRIproteiinitNMR-spektroskopiaDispersion (chemistry)Peptide sequenceresonance assignmentSpectroscopy030304 developmental biologyJournal of Biomolecular NMR
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A novel intrinsically disordered outer membrane lipoprotein ofAggregatibacter actinomycetemcomitansbinds various cytokines and plays a role in biofil…

2017

Intrinsically disordered proteins (IDPs) do not have a well-defined and stable 3-dimensional fold. Some IDPs can function as either transient or permanent binders of other proteins and may interact with an array of ligands by adopting different conformations. A novel outer membrane lipoprotein, bacterial interleukin receptor I (BilRI) of the opportunistic oral pathogen Aggregatibacter actinomycetemcomitans binds a key gatekeeper proinflammatory cytokine interleukin (IL)-1b. Because the amino acid sequence of the novel lipoprotein resembles that of fibrinogen binder A of Haemophilus ducreyi, BilRI could have the potential to bind other proteins, such as host matrix proteins. However, from th…

outer membrane lipoproteinsbacterial cytokine receptorbiofilm matrix composition0301 basic medicineMicrobiology (medical)Virulence FactorsLipoproteinsInterleukin-1beta030106 microbiologyImmunologyGingivaBiologyIntrinsically disordered proteinsAggregatibacter actinomycetemcomitansMicrobiologybacterial cytokine receptors03 medical and health sciencesHumansInterleukin 8Periodontal Diseasesouter membrane lipoproteinTumor Necrosis Factor-alphaInterleukin-8ta1182Biochemistry and Molecular BiologyBiofilmAggregatibacter actinomycetemcomitansReceptors Interleukin-1food and beveragesintrinsically disordered proteinbiology.organism_classificationInterleukin-10Cell biologyIntrinsically Disordered ProteinsInterleukin 10EditorialInfectious DiseasesBiochemistryBiofilmsParasitologyTumor necrosis factor alphabiofilm matrix compositionsintrinsically disordered proteinsBacterial outer membraneBiokemi och molekylärbiologiResearch PaperBacterial Outer Membrane ProteinsLipoproteinVirulence
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Decreased temperature increases the expression of a disordered bacterial late embryogenesis abundant (LEA) protein that enhances natural transformati…

2021

Late embryogenesis abundant (LEA) proteins are important players in the management of responses to stressful conditions, such as drought, high salinity, and changes in temperature. Many LEA proteins do not have defined three-dimensional structures, so they are intrinsically disordered proteins (IDPs) and are often highly hydrophilic. Although LEA-like sequences have been identified in bacterial genomes, the functions of bacterial LEA proteins have been studied only recently. Sequence analysis of outer membrane interleukin receptor I (BilRI) from the oral pathogen Aggregatibacter actinomycetemcomitans indicated that it shared sequence similarity with group 3/3b/4 LEA proteins. Comprehensive …

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