Search results for "folding"

showing 10 items of 330 documents

The tetrameric α-helical membrane protein GlpF unfolds via a dimeric folding intermediate.

2011

Many membrane proteins appear to be present and functional in higher-order oligomeric states. While few studies have analyzed the thermodynamic stability of α-helical transmembrane (TM) proteins under equilibrium conditions in the past, oligomerization of larger polytopic monomers has essentially not yet been studied. However, it is vital to study the folding of oligomeric membrane proteins to improve our understanding of the general mechanisms and pathways of TM protein folding. To investigate the folding and stability of the aquaglyceroporin GlpF from Escherichia coli, unfolding of the protein in mixed micelles was monitored by steady-state fluorescence and circular dichroism spectroscopy…

Gel electrophoresisCircular dichroismProtein FoldingChemistryCircular DichroismEscherichia coli ProteinsMembrane ProteinsAquaporinsBiochemistryMicelleTransmembrane proteinProtein Structure SecondaryFolding (chemistry)CrystallographyKineticsMembrane proteinBiophysicsEscherichia coliProtein foldingChemical stabilityDimerizationProtein UnfoldingBiochemistry
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Structural stability and properties of three isoforms of the major light-harvesting chlorophyll a/b complexes of photosystem II.

2008

AbstractThree isoforms of the major light-harvesting chlorophyll (Chl) a/b complexs of photosystem II (LHCIIb) in the pea, namely, Lhcb1, Lhcb2, and Lhcb3, were obtained by overexpression of apoprotein in Escherichia coli and by successfully refolding these isoforms with thylakoid pigments in vitro. The sequences of the protein, pigment stoichiometries, spectroscopic characteristics, thermo- and photostabilities of different isoforms were analysed. Comparison of their spectroscopic properties and structural stabilities revealed that Lhcb3 differed strongly from Lhcb1 and Lhcb2 in both respects. It showed the lowest Qy transition energy, with its reddest absorption about 2 nm red-shifted, an…

Gene isoformChlorophyllChlorophyll aProtein FoldingPhotosystem IIBiophysicsLight-Harvesting Protein ComplexesPhotochemistryBiochemistryThylakoidsReconstitutionchemistry.chemical_compoundPigmentPigment stoichiometryEscherichia coliThermal stabilityMajor light-harvesting chlorophyll a/b complex of photosystem IIProtein Structure QuaternaryThermostabilityPlant ProteinsChlorophyll APeasPhotosystem II Protein ComplexCell BiologyRecombinant ProteinsIsoenzymeschemistryPhotostabilityChlorophyllThylakoidvisual_artBiophysicsvisual_art.visual_art_mediumThermostabilityBiochimica et biophysica acta
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The potential of temporal analysis: Combining log data and lag sequential analysis to investigate temporal differences between scaffolded and non-sca…

2020

This paper contributes to the ongoing discussion about analysing the temporal aspects of learning processes in the educational technology research field. Our main aim was to advance methods for analysing temporal aspects of technology-enhanced learning (TEL) processes by introducing the temporal lag sequential analysis (TLSA) technique and by combining TLSA with temporal log data analysis (TLDA). Our secondary aim was to illustrate the potential of these two analysis techniques to reveal the differences between the face-to-face technology-enhanced collaborative inquiry-based learning (CIBL) processes of three different conditions (non-scaffolded, writing scaffolded and script scaffolded gro…

General Computer ScienceComputer sciencescaffoldingcomputer.software_genre050105 experimental psychologyField (computer science)Computer-Supported Collaborative LearningEducationMoodleLog datatietokoneavusteinen oppiminentechnology-enhanced inquiry0501 psychology and cognitive sciencesyhteisöllinen oppiminenlag sequential analysisbusiness.industryGroup (mathematics)05 social sciencesEducational technology050301 educationIntelligent Tutoring SystemsLag sequential analysisAsynchronous communicationpostsecondary educationkorkeakouluopiskeluInquiry-based learningScreen captureArtificial intelligencebusinesscooperative/collaborative learning0503 educationcomputeroppimisprosessiNatural language processingComputers & Education
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A Novel 1,4-Dihydropyridine Derivative Improves Spatial Learning and Memory and Modifies Brain Protein Expression in Wild Type and Transgenic APPSweD…

2015

Ca2+ blockers, particularly those capable of crossing the blood-brain barrier (BBB), have been suggested as a possible treatment or disease modifying agents for neurodegenerative disorders, e.g., Alzheimer's disease. The present study investigated the effects of a novel 4-(N-dodecyl) pyridinium group-containing 1,4-dihydropyridine derivative (AP-12) on cognition and synaptic protein expression in the brain. Treatment of AP-12 was investigated in wild type C57BL/6J mice and transgenic Alzheimer's disease model mice (Tg APPSweDI) using behavioral tests and immunohistochemistry, as well as mass spectrometry to assess the blood-brain barrier (BBB) penetration. The data demonstrated the ability …

Genetically modified mouseMalePathologymedicine.medical_specialtyDihydropyridinesTime Factorsmedicine.drug_classTransgeneSpatial Learninglcsh:MedicineMice TransgenicBlood–brain barrierAnxiolyticGyrus CinguliHippocampus03 medical and health sciences0302 clinical medicineHomer Scaffolding ProteinsMemorymedicineAnimalsHumanslcsh:Science030304 developmental biology0303 health sciencesMultidisciplinaryAmyloid beta-PeptidesGlutamate Decarboxylaselcsh:RDihydropyridineWild typeBrainmedicine.disease3. Good healthMice Inbred C57BLmedicine.anatomical_structureAnti-Anxiety AgentsBlood-Brain BarrierSynaptic plasticitylcsh:QAlzheimer's diseaseCarrier ProteinsNeuroscience030217 neurology & neurosurgerymedicine.drugResearch ArticlePloS one
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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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CO rebinding kinetics and molecular dynamics simulations highlight dynamic regulation of internal cavities in human cytoglobin

2013

Abstract: Cytoglobin (Cygb) was recently discovered in the human genome and localized in different tissues. It was suggested to play tissue-specific protective roles, spanning from scavenging of reactive oxygen species in neurons to supplying oxygen to enzymes in fibroblasts. To shed light on the functioning of such versatile machinery, we have studied the processes supporting transport of gaseous heme ligands in Cygb. Carbon monoxide rebinding shows a complex kinetic pattern with several distinct reaction intermediates, reflecting rebinding from temporary docking sites, second order recombination, and formation (and dissociation) of a bis-histidyl heme hexacoordinated reaction intermediate…

Genetics and Molecular Biology (all)ProteomicsProtein FoldingProtein ConformationMolecular biologylcsh:MedicineCrystallography X-RayLigandsBiophysics SimulationsBiochemistrychemistry.chemical_compoundProtein structureMacromolecular Structure AnalysisCinètica enzimàticaBinding Sites; Carbon Monoxide; Crystallography X-Ray; Globins; Humans; Kinetics; Ligands; Molecular Dynamics Simulation; Oxygenases; Point Mutation; Protein Binding; Protein Conformation; Medicine (all); Biochemistry Genetics and Molecular Biology (all); Agricultural and Biological Sciences (all)Biomacromolecule-Ligand Interactionslcsh:ScienceHemeCarbon MonoxideCrystallographyHemoproteinsMultidisciplinaryMedicine (all)PhysicsCytoglobinMetabolismeGlobinsBiochemistryOxygenasesddc:500Engineering sciences. TechnologyProtein BindingResearch ArticleBioquímicaProtein StructureBiophysicsReaction intermediateMolecular Dynamics SimulationProtein ChemistryGeneticsHumansPoint MutationGlobinProtein InteractionsBiologyBiologia molecularBinding SitesLigandCytoglobinlcsh:REnzyme kineticsOxygen transportProteinsComputational BiologyKineticsMetabolismAgricultural and Biological Sciences (all)chemistryX-RayBiophysicslcsh:QHuman medicineGenèticaCarbon monoxide
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Hsp90 dictates viral sequence space by balancing the evolutionary tradeoffs between protein stability, aggregation and translation rate

2017

AbstractAcquisition of mutations is central to evolution but the detrimental effects of most mutations on protein folding and stability limit protein evolvability. Molecular chaperones, which suppress aggregation and facilitate polypeptide folding, are proposed to promote sequence diversification by buffering destabilizing mutations. However, whether and how chaperones directly control protein evolution remains poorly understood. Here, we examine the effect of reducing the activity of the key eukaryotic chaperone Hsp90 on poliovirus evolution. Contrary to predictions of a buffering model, inhibiting Hsp90 increases population sequence diversity and promotes accumulation of mutations reducin…

Geneticseducation.field_of_studybiologyPopulationComputational biologyProtein aggregationHsp90EvolvabilityChaperone (protein)biology.proteinProtein foldingSynonymous substitutioneducationBiogenesis
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Histone Code and Higher-Order Chromatin Folding: A Hypothesis

2016

AbstractHistone modifications alone or in combination are thought to modulate chromatin structure and function; a concept termed histone code. By combining evidence from several studies, we investigated if the histone code can play a role in higher-order folding of chromatin. Firstly using genomic data, we analyzed associations between histone modifications at the nucleosome level. We could dissect the composition of individual nucleosomes into five predicted clusters of histone modifications. Secondly, by assembling the raw reads of histone modifications at various length scales, we noticed that the histone mark relationships that exist at nucleosome level tend to be maintained at the high…

GenomicsSolenoid (DNA)Computational biologyChromatin remodelingArticleepigenetic regulationchemistry.chemical_compoundHistone H1super-resolution microscopyHistone methylationHistone H2ANucleosomeHistone codemeiosishistone modificationHistone octamerEpigeneticsGeneticsbiologynucleosomeFolding (DSP implementation)ChromatinHistonechemistrychromatin foldinghistone codebiology.proteinDNAchromatin organizationGenomics and computational biology
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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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Local dynamic properties of the heme pocket in native and solvent-induced molten-globule-like states of cytochrome c

2002

We report the Soret absorption band, down to cryogenic temperature, of native and molten-globule-like state of horse heart cytochrome c. The band profile is analyzed in terms of vibronic coupling of the heme normal modes to the electronic transition in the framework of the Franck-Condon approximation. From the temperature dependence of the Gaussian broadening and of the peak position, we obtain information on the 'bath' of low frequency harmonic motions of the heme group within the heme pocket. The reported data indicate that, compared to the native state, the less rigid tertiary structure of the molten globule is reflected in a higher flexibility of the heme pocket and in greater conformat…

GlycerolProtein FoldingHot TemperatureCytochromeProtein ConformationBiophysicsCytochrome c GroupHemeProtein dynamicsBiochemistrychemistry.chemical_compoundMolten-globule proteinsNative stateSettore BIO/10HemeBinding SitesbiologySpectrum AnalysisProtein dynamicsOrganic ChemistryMolten globuleOptical absorption spectroscopyCrystallographyVibronic couplingchemistryAbsorption bandbiology.proteinMolten-globule proteins; Optical absorption spectroscopy; Protein dynamicsProtein foldingMathematics
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