Search results for " Helix"

showing 10 items of 106 documents

Atrial fibrillation is associated with cardiac hypoxia.

2008

BACKGROUND: Atrial fibrillation (AF), the most common human arrhythmia, is responsible for substantial morbidity and mortality and may be promoted by selective atrial ischemia and atrial fibrosis. Consequently, we investigated markers for hypoxia and angiogenesis in AF. METHODS: Right atrial appendages (n=158) were grouped according to heart rhythm [sinus rhythm (SR) or AF]. The degree of fibrosis and microvessel density of all patients were determined morphometrically using Sirius-Red- and CD34/CD105-stained sections, respectively. Next, sections (n=77) underwent immunostaining to detect hypoxia- and angiogenesis-related proteins [hypoxia-inducible factor (HIF)1 alpha, HIF2 alpha, vascular…

MaleVascular Endothelial Growth Factor Amedicine.medical_specialtyCytoplasmAngiogenesisIschemiaMyocardial IschemiaBiologyPathology and Forensic Medicinechemistry.chemical_compoundFibrosisInternal medicineAtrial FibrillationmedicineBasic Helix-Loop-Helix Transcription FactorsHumansSinus rhythmAtrial AppendageHypoxiaMicrovesselAgedCell NucleusNeovascularization PathologicMicrocirculationMyocardiumAtrial fibrillationGeneral MedicineHypoxia (medical)Middle Agedmedicine.diseaseHypoxia-Inducible Factor 1 alpha SubunitCoronary VesselsFibrosisUp-RegulationVascular endothelial growth factorEndocrinologychemistryCardiologyFemalemedicine.symptomCardiology and Cardiovascular MedicineBiomarkersCardiovascular pathology : the official journal of the Society for Cardiovascular Pathology
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New Challenges of Economic and Business Development – 2012 : Conference Proceedings (May 10 - 12, 2012, Riga, University of Latvia)

2012

Support for Conference Proceedings by ERAF Project "Support for the international cooperation projects and other international cooperation activities in research and technology at the University of Latvia" No. 2010/0202/2DP/2.1.1.2.0/10/APIA/VIAA/013

Market efficiencyInternational franchisingTriple Helix modelOptimal capital structureLogisticsGDPTeam PerformanceManagement theoryTourismAirline industryStakeholdersInsurance marketsNew Product DevelopmentRisksHuman capitalMunicipality budgetMarketingDevelopment economicsResearch policyCost-benefit analysisBusiness groupsOrganizational developmentMergers and acquisitionsInternational rating agencyCompliance Management SystemsRegional integrationKnowledge sharingFinancial scienceWell-beingBargain purchaseTax wedgeFinancial managementEducationEmployee selectionMonetary policyCorporate cultureHigher educationCitizen participationInnovationMotivationOnline surveysManagement educationEmployer BrandingBrand imageFinancial analysisInternal auditPrint advertisement assessmentICT:SOCIAL SCIENCES::Business and economics [Research Subject Categories]Environmental management accountingFinancial system stabilityEmployee satisfactionBanking sectorSocial MediaPension system
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Dystopia deconstructed: Applying the triple helix model to a failed utopia

2016

This study analyzes the failure of a literary utopian system—Veronica Roth's Divergent—drawing from difference, which the divergent and the factionless represent. The analysis of the causes and consequences of difference from a socioeconomic perspective reveals a system that the triple helix model can improve. The adapted model based on cooperation and knowledge transfer adds two connections to the three main axes: Universities (Erudite), Government (Abnegation), and Industry (Amity), and gives the divergent a key role: inter-faction coordinators. Following a review of European migration policies, the study explores the creation of a new faction for the factionless. Regarding innovation, th…

MarketingGovernmentDystopiamedia_common.quotation_subject05 social sciencesPerspective (graphical)EpistemologyManagementUtopia0502 economics and business050211 marketingSociologyKnowledge transfer050203 business & managementTriple helixmedia_commonJournal of Business Research
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Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site

2003

Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an alpha/beta hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis, solved using single-wavelength anomalous dispersion from a selenomethionine-substituted protein and refined at 1.2 A resolution. This enzyme represents a completely different structure and a novel one-step mechanism. The fold features a highly curved six-stranded mixed beta-sheet, with four alpha-helices packed onto it to create a …

Models MolecularAFSG Stafafdelingen (WUATV)10050 Institute of Pharmacology and Toxicologydrug protein bindingEnantioselectivityEpoxide hydrolaseCrystallography X-Rayuncultured actinomyceteCatalytic Domain2400 General Immunology and Microbiologyalpha helixRhodococcuscholesterol epoxide hydrolasenaphthalene 12-dioxygenasedcl14limonene 12 epoxide hydrolaseEpoxide hydrolaseBacteria (microorganisms)delta(5)-3-ketosteroid isomeraseEpoxide HydrolasesLimonene-12-epoxide hydrolaseGeneral Neurosciencearticle2800 General NeuroscienceActinobacteria (class)Articlesagrobacterium-radiobacterEnzyme structureRecombinant Proteinsunclassified drugenzyme structurereaction analysisBiochemistrypriority journalenzyme active siteMechanism2-dioxygenaseDimerizationBiotechnologychemical reactioncrystal structureaspergillus-nigermacromolecular structuresStereochemistrybeta sheetvalpromideMolecular Sequence Data610 Medicine & healthGenetics and Molecular BiologyBiologyGeneral Biochemistry Genetics and Molecular BiologyBacterial Proteinssite directed mutagenesis1300 General Biochemistry Genetics and Molecular BiologyHydrolase1312 Molecular BiologyAmino Acid SequencedetoxificationRhodococcus erythropolisBiologyMonoterpene degradationMolecular Biologyprotein data-bankenzyme substrate complexEnzyme substrate complexnonhumancatalysisSequence Homology Amino AcidGeneral Immunology and Microbiologybacterial enzymeActive sitecrystal-structureAFSG Staff Departments (WUATV)enzyme metabolismProtein SubunitsenzymeEpoxide HydrolasesGeneral Biochemistrybiology.proteinMutagenesis Site-Directed570 Life sciences; biologyselenomethioninenaphthalene 1Alpha helix
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Copper(II)-Induced Restructuring of ZnuD, a Zinc(II) Transporter from Neisseria meningitidis.

2019

Cluster 2 (288HDDDNAHAHTH298) from Neisseria meningitidis ZnuD is a flexible loop that captures zinc(II) ions, acting as a "fishing net". We describe its Zn(II) and Cu(II) binding capabilities, focusing on the thermodynamics of such interactions and comparing them with the complexes of the 1MAHHHHHHL9-NH2 region. Copper(II) complexes with the studied ZnuD regions are thermodynamically more stable than the zinc(II) ones-Cu(II) complexes dominate in solution even in close to physiological ratios of the studied metal ions (a 10-fold excess of Zn(II) over Cu(II)). While the binding of native Zn(II) has no significant impact on the structure of its transporter, Cu(II) binding induces a conformat…

Models MolecularConformational changeMetal ions in aqueous solutionchemistry.chemical_elementZincNeisseria meningitidis010402 general chemistry01 natural sciencesInorganic ChemistryBacterial ProteinsHumansProlineAmino Acid SequencePhysical and Theoretical ChemistryCation Transport ProteinsPolyproline helix010405 organic chemistryTransporterCopper0104 chemical sciencesMeningococcal InfectionsCrystallographyZincchemistryHelixThermodynamicsCopperProtein BindingInorganic chemistry
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Conformational and structural analysis of the equilibrium between single- and double-strand ?-helix of aD,L-alternating oligonorleucine

2004

Alternating sequences of D and L residues in peptides are directly related to the formation of several kinds of regular helical conformations usually called beta-helices. The major feature of these structures is that they can be associated with the transmembrane ion-conducting channel activity in some natural antibacterial peptides. The study of alternating D,L synthetic peptides is critical to understand how factors such as surrounding media, main chain length, type of side chain and terminal groups, among others, can determine the adoption of a specific kind of beta-helix. Early studies pointed out that the peptides Boc-(D-NLeu-L-NLeu)(6)-D-MeNLe-L-Nl-D-Nl-L-Nl-OMe (Boc: tert-butyloxycarb…

Models MolecularMagnetic Resonance SpectroscopyProtein ConformationStereochemistryDimerMolecular Sequence DataBiophysicsDNA Single-StrandedBeta helixStereoisomerismAntiparallel (biochemistry)BiochemistryProtein Structure SecondaryBiomaterialsMolecular dynamicschemistry.chemical_compoundProtein structureNorleucineSide chainAmino Acid SequenceChemistryOrganic ChemistryStereoisomerismDNAGeneral MedicineNuclear magnetic resonance spectroscopyCrystallographyNucleic Acid ConformationThermodynamicsOligopeptidesBiopolymers
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A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer

2012

AbstractWhen localized adjacent to a Pro-kink, Thr and Ser residues can form hydrogen bonds between their polar hydroxyl group and a backbone carbonyl oxygen and thereby modulate the actual bending angle of a distorted transmembrane α-helix. We have used the homo-dimeric transmembrane cytochrome b559′ to analyze the potential role of a highly conserved Ser residue for assembly and stabilization of transmembrane proteins. Mutation of the conserved Ser residue to Ala resulted in altered heme binding properties and in increased stability of the holo-protein, most likely by tolerating subtle structural rearrangements upon heme binding. The results suggest a crucial impact of an intrahelical Ser…

Models MolecularProlineHeme bindingStereochemistryDimerMolecular ConformationBiophysicsCofactor bindingHemeBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureProtein stabilitySerineProtein foldingCofactor bindingHydrogen bondCell MembranePhotosystem II Protein ComplexHydrogen BondingCell BiologyCytochrome b GroupTransmembrane proteinProtein Structure TertiaryOxygenTransmembrane domainHelix interactionchemistrySpectrophotometryMembrane proteinMutationTransmembrane helixProtein foldingDimerizationProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Influence of proline residues in transmembrane helix packing

2003

Integral membrane proteins often contain proline residues in their alpha-helical transmembrane (TM) fragments, which may strongly influence their folding and association. Pro-scanning mutagenesis of the helical domain of glycophorin A (GpA) showed that replacement of the residues located at the center abrogates helix packing while substitution of the residues forming the ending helical turns allows dimer formation. Synthetic TM peptides revealed that a point mutation of one of the residues of the dimerization motif (L75P) located at the N-terminal helical turn of the GpA TM fragment, adopts a secondary structure and oligomeric state similar to the wild-type sequence in detergents. In additi…

Models MolecularProtein FoldingGlycosylationProlineStereochemistryProtein ConformationCollagen helixRecombinant Fusion ProteinsMolecular Sequence DataEndoplasmic ReticulumProtein Structure SecondaryComputers MolecularProtein structureStructural BiologyAmino Acid SequenceGlycophorinsMolecular BiologyIntegral membrane proteinProtein secondary structureChemistryCell MembraneProteïnes de membranaWaterLipidsTransmembrane proteinPeptide FragmentsCrystallographyTransmembrane domainMembrane proteinHelixMutagenesis Site-DirectedDimerization
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Mona/Gads SH3C binding to hematopoietic progenitor kinase 1 (HPK1) combines an atypical SH3 binding motif, R/KXXK, with a classical PXXP motif embedd…

2004

Hematopoietic progenitor kinase 1 (HPK1) is implicated in signaling downstream of the T cell receptor. Its non-catalytic, C-terminal half contains several prolinerich motifs, which have been shown to interact with different SH3 domain-containing adaptor proteins in vitro. One of these, Mona/Gads, was also shown to bind HPK1 in mouse T cells in vivo. The region of HPK1 that binds to the Mona/Gads C-terminal SH3 domain has been mapped and shows only very limited similarity to a recently identified high affinity binding motif in SLP-76, another T-cell adaptor. Using isothermal titration calorimetry and x-ray crystallography, the binding of the HPK1 motif to Mona/Gads SH3C has now been characte…

Models MolecularTime FactorsProtein ConformationAmino Acid MotifsMolecular Sequence DataPlasma protein bindingBiologyCalorimetryProtein Serine-Threonine KinasesCrystallography X-RayBiochemistrySH3 domainProtein Structure Secondarysrc Homology DomainsMiceProtein structureAnimalsHumansAmino Acid SequenceMolecular BiologyPeptide sequencePolyproline helixAdaptor Proteins Signal TransducingSequence Homology Amino AcidSignal transducing adaptor proteinIsothermal titration calorimetryCell BiologyPhosphoproteinsCell biologyProtein Structure TertiaryCrystallographyKineticsPXXP MotifCarrier ProteinsPeptidesProtein BindingThe Journal of biological chemistry
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Solution structure of aD,L-alternating oligonorleucine as a model of double-stranded antiparallel ?-helix

2002

Conformational characteristics of alternating D,L linear peptides are of particular interest because of their capacity to form transmembrane channels with different transport properties, as some natural antibiotics do. Single- and double-stranded beta-helical structures are common for alternating D,L peptides. The stability of the beta-helix depends on several structural factors, such as the backbone peptide length, type and position of side chains, and nature of terminal groups. The NMR and molecular dynamics solution conformation of a synthetic alternating D,L-oligopeptide with 15 norleucines (XVMe) has been used as a model to get insight in to the conformational features of double-strand…

Models Molecularenergy minimizationStereochemistryBiophysicsBeta helixStereoisomerismEnergy minimizationAntiparallel (biochemistry)BiochemistryProtein Structure SecondaryBiomaterialsMolecular dynamicsBiopolymerstwo-dimensional NMRProtein structureNorleucineSide chainDL-alternating peptNuclear Magnetic Resonance BiomolecularTransmembrane channelsChemistryOrganic ChemistryStereoisomerismGeneral Medicinemolecular dynamicsCrystallographybeta-helixOligopeptidesBiopolymers
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