Search results for "Timer"

showing 10 items of 119 documents

Detergent Properties Influence the Stability of the Glycophorin A Transmembrane Helix Dimer in Lysophosphatidylcholine Micelles

2012

AbstractDetergents might affect membrane protein structures by promoting intramolecular interactions that are different from those found in native membrane bilayers, and fine-tuning detergent properties can be crucial for obtaining structural information of intact and functional transmembrane proteins. To systematically investigate the influence of the detergent concentration and acyl-chain length on the stability of a transmembrane protein structure, the stability of the human glycophorin A transmembrane helix dimer has been analyzed in lyso-phosphatidylcholine micelles of different acyl-chain length. While our results indicate that the transmembrane protein is destabilized in detergents w…

DetergentsMolecular Sequence DataBiophysicsMicelleProtein Structure SecondaryCell membraneHydrophobic mismatchmedicineHumansGlycophorinAmino Acid SequenceGlycophorinsLipid bilayerMicellesAggregation numberDose-Response Relationship DrugbiologyChemistryCell MembraneMembraneLysophosphatidylcholinesTransmembrane proteinTransmembrane domainmedicine.anatomical_structureBiochemistrybiology.proteinBiophysicslipids (amino acids peptides and proteins)Protein MultimerizationHydrophobic and Hydrophilic InteractionsBiophysical Journal
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Unfolding a transmembrane helix dimer: A FRET study in mixed micelles

2009

The exact nature of membrane protein folding and assembly is not understood in detail yet. Addition of SDS to a membrane protein dissolved in mild, non-polar detergent results in formation of mixed micelles and in subsequent denaturation of higher ordered membrane protein structures. The exact nature of this denaturation event is, however, enigmatic, and separation of an individual helix pair in mixed micelles has also not been reported yet. Here we followed unfolding of the human glycophorin A transmembrane helix dimer in mixed micelles by fluorescence spectroscopy. Energy transfer between differently labelled glycophorin A transmembrane helices decreased with increasing SDS mole fractions…

DimerBiophysicsBiochemistryMicelleProtein Structure SecondarySurface-Active Agentschemistry.chemical_compoundFluorescence Resonance Energy TransferHumansGlycophorinGlycophorinsMolecular BiologyMicellesbiologyChemistryPeripheral membrane proteinSodium Dodecyl SulfateTransmembrane proteinProtein Structure TertiaryKineticsTransmembrane domainCrystallographyFörster resonance energy transferMembrane proteinbiology.proteinProtein MultimerizationArchives of Biochemistry and Biophysics
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Decidability of bisimulation equivalences for parallel timer processes

1993

In this paper an abstract model of parallel timer processes (PTPs), allowing specification of temporal quantitative constraints on the behaviour of real time systems, is introduced. The parallel timer processes are defined in a dense time domain and are able to model both concurrent (with delay intervals overlapping on the time axis) and infinite behaviour. Both the strong and weak (abstracted from internal actions) bisimulation equivalence problems for PTPs are proved decidable. It is proved also that, if one provides the PTP model additionally with memory cells for moving timer value information along the time axis, the bisimulation equivalence (and even the vertex reachability) problems …

Discrete mathematicsCounter machineBisimulationVertex (graph theory)ReachabilityComputer scienceTime domainTimerAlgorithmUndecidable problemDecidability
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Adaptation and ecological speciation in seasonally varying environments at high latitudes: Drosophila virilis group

2022

Living in high latitudes and altitudes sets specific requirements on species’ ability to forecast seasonal changes and to respond to them in an appropriate way. Adaptation into diverse environmental conditions can also lead to ecological speciation through habitat isolation or by inducing changes in traits that influence assortative mating. In this review, we explain how the unique time-measuring systems of Drosophila virilis group species have enabled the species to occupy high latitudes and how the traits involved in species reproduction and survival exhibit strong linkage with latitudinally varying photoperiodic and climatic conditions. We also describe variation in reproductive barriers…

Drosophila virilis groupReproductive IsolationmahlakärpäsetGenetic SpeciationLocal adaptationPhotoperiodreproductive diapauseReviewkylmänkestävyysphotoperiodic timerchromosomal inversionscircadian clockilmastoelinympäristöAnimalsmuuntelu (biologia)lepotilavuorokausirytmisopeutuminenvuodenajatkromosomi-inversiotReproductioncold tolerancelisääntyminenAdaptation Physiologicalgenome sequencingInsect SciencelajiutuminenDrosophilacandidate genesreproductive barrierslocal adaptationFly
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Crystal structure of human gamma-butyrobetaine hydroxylase.

2010

Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of gamma-butyrobetaine (GBB). l-carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy. The only known synthetic inhibitor of GBBH is mildronate (3-(2,2,2-trimethylhydrazinium) propionate dihydrate), which is a non-hydroxylatable analog of GBB. To aid in the discovery of novel GBBH inhibitors by rational drug design, we have solved the three-dimensional structure of recombinant human GBBH at 2.0A resolution. The GBBH monomer consists of a catalytic double-stranded beta-helix (DBSH) domai…

EGF-like domainStereochemistrygamma-Butyrobetaine DioxygenaseBiophysicsDrug designBiochemistryHydroxylationchemistry.chemical_compoundDioxygenaseCatalytic DomainHumansEnzyme InhibitorsMolecular BiologyHistidinechemistry.chemical_classificationCrystallographybiologyActive siteCell BiologyRecombinant ProteinsZincEnzymeBiochemistrychemistryCyclic nucleotide-binding domainDrug Designbiology.proteinProtein MultimerizationMethylhydrazinesBiochemical and biophysical research communications
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Microfinance Mission Drift?

2010

Claims have been made that microfinance institutions (MFIs) experience mission drift as they increasingly cater to customers who are better off than their original customers. We investigate mission drift using average loan size as a main proxy and the MFI?s lending methodology, main market, and gender bias as further mission drift measures. We employ a large data set of rated, multi-country MFIs spanning 11 years, and perform panel data estimations with instruments. We find that the average loan size has not increased in the industry as a whole, nor is there a tendency towards more individual loans or a higher proportion of lending to urban costumers. Regressions show that an increase in av…

Economics and EconometricsMicrofinanceActuarial scienceSociology and Political ScienceVDP::Samfunnsvitenskap: 200::Økonomi: 210::Bedriftsøkonomi: 213:Samfunnsvitenskap: 200::Økonomi: 210::Bedriftsøkonomi: 213 [VDP]Geography Planning and DevelopmentMicrofinanceDevelopmentlaw.inventionGMM estimationlawEstimeringEconomicsDouble bottom linePostprintMission driftEstimationPanel dataPanel data
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Oligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesterol-dependent cytolysin

2013

Pyolysin (PLO) belongs to the homologous family of the cholesterol- dependent cytolysins (CDCs), which bind to cell membranes containing cholesterol to form oligomeric pores of large size. The CDC monomer structure consists of 4 domains. Among these, the C-terminal domain 4 has been implicated in membrane binding of the monomer, while the subsequent processes of oligomerization and membrane insertion have primarily been assigned to other domains of the molecule. Recombinantly expressed or proteolytic fragments that span domain 4 of the CDCs streptolysin O and perfringolysin O bind to membranes but fail to oligomerize, and they inhibit the activity of the respective wild-type toxins. We repo…

ErythrocytesMembrane bindingCellprotein bindingBiochemistryoligomerHemolysin Proteinschemistry.chemical_compoundReaction kineticsToxic materialsMonomersprotein domainRecombinant ProteinsHemolysisunclassified drugcytolysinmedicine.anatomical_structureMembraneBiochemistryStreptolysinsStreptolysinLarge sizeBacterial ToxinsBiologyCholesterol-dependent cytolysinHemolysisoligomerizationMembrane LipidsBacterial ProteinsProteolytic fragmentsEscherichia colimedicineAnimalsMonomer structuresMolecular BiologySheep Domesticcarboxy terminal sequenceC-terminal domainsCholesterolC-terminusCell MembraneHemolytic activitycholesterolCell Biologymedicine.diseaseProtein Structure TertiaryCell membranesKineticschemistryOligomersProtein MultimerizationPyolysinprotein pyolysinMembrane insertionCytology
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Wild-type Cu/Zn superoxide dismutase stabilizes mutant variants by heterodimerization

2014

Mutations in the gene encoding Cu/Zn superoxide dismutase (SOD1) are responsible for a subset of amyotrophic lateral sclerosis cases presumably by the acquisition of as yet unknown toxic properties. Additional overexpression of wild-type SOD1 in mutant SOD1 transgenic mice did not improve but rather accelerated the disease course. Recently, it was documented that the presence of wild-type SOD1 (SOD(WT)) reduced the aggregation propensity of mutant SOD1 by the formation of heterodimers between mutant and SOD1(WT) and that these heterodimers displayed at least a similar toxicity in cellular and animal models. In this study we investigated the biochemical and biophysical properties of obligate…

Genetically modified mouseanimal diseasesMutantSOD1HeterodimerizationPeptideBiologyProtein aggregationlcsh:RC321-571Superoxide Dismutase-1Humanslcsh:Neurosciences. Biological psychiatry. NeuropsychiatryGenechemistry.chemical_classificationMisfoldingSuperoxide DismutaseWild typenutritional and metabolic diseasesSOD1Molecular biologynervous system diseasesHEK293 Cellsnervous systemNeurologychemistryBiochemistryDismutase activityMutationDismutaseProtein aggregationProtein MultimerizationMutant homodimersNeurobiology of Disease
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Thermal aggregation of glycated bovine serum albumin

2010

International audience; Aggregation and glycation processes in proteins have a particular interest in medicine fields and in food technology. Serum albumins are model proteins which are able to self-assembly in aggregates and also sensitive to a non-enzymatic glycation in cases of diabetes. In this work, we firstly reported a study on the glycation and oxidation effects on the structure of bovine serum albumin (BSA). The experimental approach is based on the study of conformational changes of BSA at secondary and tertiary structures by FTIR absorption and fluorescence spectroscopy, respectively. Secondly, we analysed the thermal aggregation process on BSA glycated with different glucose con…

Glycation End Products AdvancedGlycosylationHot TemperatureGlycoxidation02 engineering and technologyProtein aggregationBiochemistryProtein Structure SecondaryAnalytical Chemistrychemistry.chemical_compoundProtein structureGlycationSpectroscopy Fourier Transform InfraredScattering RadiationGlycated Serum AlbuminBovine serum albuminGlycation0303 health sciencesbiologyChemistryTryptophanSerum Albumin Bovine021001 nanoscience & nanotechnology3. Good healthSpectrophotometryProtein aggregation0210 nano-technologyOxidation-ReductionGlycosylationBiophysicsSerum albuminIn Vitro Techniques03 medical and health sciencesAnimalsMolecular BiologySerum Albumin030304 developmental biologyChromatographyAlbuminAlbuminLight scatteringSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein tertiary structureProtein Structure TertiaryKineticsFTIR spectroscopyGlucoseSpectrometry FluorescenceUnfolded Protein Responsebiology.proteinCattleProtein Multimerization[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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The GlpF residue Trp219 is part of an amino-acid cluster crucial for aquaglyceroporin oligomerization and function

2018

The vestibule loop regions of aquaglyceroporins are involved in accumulation of glycerol inside the channel pore. Even though most loop regions do not show high sequence similarity among aquaglyceroporins, loop E is highly conserved in aquaglyceroporins, but not in members of the homologous aquaporins. Specifically, a tryptophan residue is extremely conserved within this loop. We have investigated the role of this residue (Trp219) that deeply protrudes into the protein and potentially interacts with adjacent loops, using the E. coli aqualgyeroporin GlpF as a model. Replacement of Trp219 affects the activity of GlpF and impairs the stability of the tetrameric protein. Furthermore, we have id…

GlycerolModels Molecular0301 basic medicineProtein ConformationTetrameric proteinBiophysicsAquaporinAquaporinsBiochemistry03 medical and health sciencesResidue (chemistry)TetramerEscherichia coliAmino Acidschemistry.chemical_classification030102 biochemistry & molecular biologyProtein StabilityChemistryEscherichia coli ProteinsTryptophanTryptophanCell BiologyAmino acid030104 developmental biologyAquaglyceroporinsBiochemistryMutationBiophysicsProtein foldingProtein MultimerizationAquaglyceroporinsBiochimica et Biophysica Acta (BBA) - Biomembranes
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