Search results for "oligo"

showing 10 items of 1298 documents

Mechanism of Oligomerisation of Cyclase-associated Protein from Dictyostelium discoideum in Solution

2006

Abstract Cyclase-associated protein (CAP) is a highly conserved modular protein implicated in the regulation of actin filament dynamics and a variety of developmental and morphological processes. The protein exists as a high molecular weight complex in cell extracts and purified protein possesses a high tendency to aggregate, a major obstacle for crystallisation. Using a mutagenesis approach, we show that two structural features underlie the mechanism of oligomerisation in Dictyostelium discoideum CAP. Positively charged clusters on the surface of the N-terminal helix-barrel domain are involved in inter-molecular interactions with the N or C-terminal domains. Abolishing these interactions m…

Models MolecularProtein DenaturationProtein FoldingProtein ConformationMolecular Sequence DataOligomerDictyostelium discoideumMass SpectrometryProtein Structure SecondaryProtein–protein interactionProtein filamentchemistry.chemical_compoundProtein structureStructural BiologyEnzyme StabilityAnimalsUreaDictyosteliumAmino Acid SequenceMolecular BiologyActinN capCrystallographybiologyCircular Dichroismbiology.organism_classificationDictyosteliumActinsProtein Structure TertiaryMolecular WeightSolutionsCytoskeletal ProteinschemistryBiochemistryModels ChemicalMutationBiophysicsChromatography GelDimerizationProtein Binding
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Single-Molecule FRET Reveals a Cooperative Effect of Two Methyl Group Modifications in the Folding of Human Mitochondrial tRNALys

2011

Summary Using a combination of advanced RNA synthesis techniques and single molecule spectroscopy, the deconvolution of individual contributions of posttranscriptional modifications to the overall folding and stabilization of human mitochondrial tRNA Lys is described. An unexpected destabilizing effect of two pseudouridines on the native tRNA folding was evidenced. Furthermore, the presence of m 2 G10 alone does not facilitate the folding of tRNA Lys , but a stabilization of the biologically functional cloverleaf shape in conjunction with the principal stabilizing component m 1 A9 exceeds the contribution of m 1 A alone. This constitutes an unprecedented cooperative effect of two nucleotide…

Models MolecularRNA StabilityMolecular Sequence DataClinical BiochemistryContext (language use)BiologyBiochemistryOrganophosphorus CompoundsDrug DiscoveryFluorescence Resonance Energy TransferHumansNucleotideMagnesiumTRNA foldingColoring AgentsMolecular Biologychemistry.chemical_classificationPharmacologyBase SequenceOligonucleotideRNAGeneral MedicineSingle-molecule FRETMitochondriaFolding (chemistry)chemistryBiochemistryTransfer RNABiophysicsNucleic Acid ConformationRNA Transfer LysMolecular MedicinePseudouridineChemistry & Biology
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Functional competition within a membrane: Lipid recognition vs. transmembrane helix oligomerization

2015

Abstract Binding of specific lipids to large, polytopic membrane proteins is well described, and it is clear that such lipids are crucial for protein stability and activity. In contrast, binding of defined lipid species to individual transmembrane helices and regulation of transmembrane helix monomer–oligomer equilibria by binding of distinct lipids is a concept, which has emerged only lately. Lipids bind to single-span membrane proteins, both in the juxta-membrane region as well as in the hydrophobic membrane core. While some interactions counteract transmembrane helix oligomerization, in other cases lipid binding appears to enhance oligomerization. As reversible oligomerization is involve…

Models MolecularSyntaxin 1AMembrane lipidsLipid BilayersBiophysicsBiologyBinding CompetitiveBiochemistryProtein Structure SecondaryMembrane LipidsLipid bindingOligomerizationIntegral membrane proteinC99Transmembrane channelsMolecular StructureMembrane transport proteinCell MembranePeripheral membrane proteinMembrane ProteinsCell Biologyp24Transmembrane proteinProtein Structure TertiaryCell biologyTransmembrane domainMembrane proteinMembrane proteinbiology.proteinlipids (amino acids peptides and proteins)Protein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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A molecular assembly system that renders antigens of choice highly repetitive for induction of protective B cell responses.

2002

Virus like particles (VLPs) are known to induce potent B cell responses in the absence of adjuvants. Moreover, epitope-specific antibody responses may be induced by VLPs that contain peptides inserted in their immunodominant regions. However, due to steric problems, the size of the peptides capable of being incorporated into VLPs while still permitting capsid assembly, is rather limited. While peptides genetically fused to either the N- or C-terminus of VLPs present fewer assembly problems, the immune responses obtained against such epitopes are often limited, most likely because the epitopes are not optimally exposed. In addition, such particles may be less stable in vivo. Here, we show th…

Models MolecularViral Hepatitis VaccinesHepatitis B virusMacromolecular SubstancesProtein ConformationvirusesRecombinant Fusion ProteinsProtozoan ProteinsAntigens ProtozoanBiologyProtein EngineeringEpitopePhospholipases AInclusion Bodies ViralViral Matrix ProteinsMiceImmune systemAntigenVirus-like particlemedicineAnimalsB cellB-LymphocytesMice Inbred BALB CVaccines SyntheticGeneral VeterinaryGeneral Immunology and MicrobiologyImmunodominant EpitopesImmunogenicityVaccinationPublic Health Environmental and Occupational HealthMolecular biologyHepatitis B Core AntigensPeptide FragmentsCell biologyProtein Structure TertiaryHBcAgBee VenomsInfectious Diseasesmedicine.anatomical_structureCross-Linking ReagentsCapsidDrug DesignMolecular MedicineFemaleImmunizationPeptidesOligopeptidesVaccine
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N-[tert-Butoxycarbonylglycyl-(Z)-α,β-dehydrophenylalanylglycyl-(E)-α,β-dehydrophenylalanylphenylalanyl]-4-nitroaniline ethanol solvate

2005

The alpha,beta-dehydrophenylalanine residues influence the conformation of the title pentapeptide Boc0-Gly1-Delta(Z)Phe2-Gly3-Delta(E)Phe4-L-Phe5-p-NA ethanol solvate, C42H43N7O9.C2H5OH. The first unsaturated phenylalanyl (Delta(Z)Phe2) and the third glycyl (Gly3) residues form a type I beta turn, while the second unsaturated phenylalanyl (Delta(E)Phe4) and the last phenylalanyl (L-Phe5) residues are part of a type II beta turn. All the amino acids in the peptide are linked trans to one another. The crystal structure is stabilized by intra- and intermolecular hydrogen bonds.

Models Molecularchemistry.chemical_classificationOligopeptideAniline CompoundsEthanolMolecular StructureHydrogen bondStereochemistryPeptideGeneral MedicineCrystal structureCrystallography X-RayPentapeptide repeatGeneral Biochemistry Genetics and Molecular BiologyAmino acidchemistry.chemical_compoundchemistryMoleculeOligopeptidesActa Crystallographica Section C Crystal Structure Communications
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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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Monoclonal antibody to a DNA-binding domain of p53 mimics charge structure of DNA: anti-idiotypes to the anti-p53 antibody are anti-DNA

2004

Antibodies to DNA are important markers of various autoimmune diseases and can be pathogenic; however, their generation is not understood. We previously reported that anti-DNA antibodies could be induced in mice by idiotypic immunization to PAb-421, an antibody to a DNA-binding domain of p53. We now report that two monoclonal antibodies of moderate affinity (K(D) asymptotically equal to 10(-7)), raised from PAb-421-immunized mice, specifically recognized both PAb-421 and DNA. These antibodies feature multiple arginine residues in the antigen-binding site, a unique characteristic of disease-associated anti-DNA antibodies; nevertheless, these anti-DNA antibodies show specific complementarity …

Models Molecularmedicine.drug_classMolecular Sequence DataImmunologyOligonucleotidesMonoclonal antibodyMicechemistry.chemical_compoundImmunoglobulin IdiotypesmedicineAnimalsImmunology and AllergyA-DNAAmino Acid SequencebiologyOligonucleotideAntibodies MonoclonalDNAMolecular biologyPrimary and secondary antibodiesProtein Structure TertiarychemistryMonoclonalbiology.proteinTumor Suppressor Protein p53AntibodyDNAProtein BindingBinding domainEuropean Journal of Immunology
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Frequency and characteristics of tooth agenesis among an orthodontic patient population

2009

Purpose: The objectives of this study were to investigate the prevalence and characteristics of tooth agenesis and the associated skeletal morphology and arch widths in a group of Turkish patients seeking orthodontic treatment. Material and Methods: We designed a retrospective study composed of pre- and post-treatment panoramic radiographs and lateral cephalometric films of 3,341 patients (2,040 females and 1,301 males). Tooth agenesis was evaluated for hypodontia and oligodontia -excluding the third molars- from the orthopantomograms. The significance test for the differences in the skeletal morphology between hypodontia and non-hypodontia patients was performed using the Pearson chi-squar…

MolarAdultMaleAdolescentTurkeyDentistryOrthodonticsOligodontiaYoung Adultstomatognathic systemmedicinePrevalenceHumansMaxillary central incisorChildGeneral DentistryAnodontiaRetrospective StudiesOrthodonticsbusiness.industryRetrospective cohort studymedicine.disease:CIENCIAS MÉDICAS [UNESCO]HypodontiaPatient populationstomatognathic diseasesOtorhinolaryngologyUNESCO::CIENCIAS MÉDICASSurgeryFemaleTooth agenesisbusiness
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Caspase-mediated apoptosis in sponges: cloning and function of the phylogenetic oldest apoptotic proteases from Metazoa

2003

AbstractSponges (phylum Porifera) represent the phylogenetically oldest metazoan phylum. These animals have complex cell adhesion and powerful immune systems which allow the formation of a distinct body plan. Consequently, an apoptotic machinery has to be predicted that allows sponges to eliminate unwanted cells accumulating during development. With the marine sponge Geodia cydonium, it is shown that allografts of these animals undergo apoptosis as demonstrated by apoptotic DNA fragmentation. Extracts from allografts contain an enzymic activity characteristic for caspases; as substrate to determine the cleavage activity, Ac-DEVD-AMC was applied. cDNAs encoding predicted caspase-3-related pr…

Molecular Sequence DataApoptosisCaspase 3SpongeCoumarinsEndopeptidasesAnimalsInvertebrateAmino Acid SequenceCloning MolecularEnzyme InhibitorsMolecular BiologyPhylogenyCaspasebiologyCaspase 3Cell adhesion moleculeAlternative splicingApoptotic DNA fragmentationPotential proapoptotic molecule DD2Cell BiologyBcl-2 homologous proteinbiology.organism_classificationSuberites domunculaCaspaseCaspase InhibitorsPoriferaCell biologyIsoenzymesSuberites domunculaSpongeApoptosisCaspasesbiology.proteinOligopeptidesSequence AlignmentBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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The membrane distal half of gp130 is responsible for the formation of a ternary complex with IL-6 and the IL-6 receptor

1995

AbstractGp130 is the signal transducing subunit of the interleukin-6 receptor. Signaling is initiated by the complex formation of gp130 with IL-6 bound to the IL-6 receptor (IL-6R). We have subdivided the extracellular domain of gp130 in two parts and expressed the mutant proteins as soluble IgG fusion proteins in COS-7 cells. By studying the formation of the ternary complex we show that the membrane distal half of gp130 which contains a cytokine receptor domain is responsible for the interaction with the IL-6/IL-6R complex. Interestingly this is the same region which is believed to be involved in specific recognition of the related cytokines LIF, OM, and probably also of CNTF and IL-11.

Molecular Sequence DataBiophysicsBiologyBiochemistryCytokine receptor domainCell Linegp130Structure-function analysisAntigens CDStructural BiologyCytokine Receptor gp130GeneticsAnimals5-HT5A receptorReceptorMolecular BiologyTernary complexMembrane GlycoproteinsBase SequenceInterleukin-6digestive oral and skin physiologyHaplorhiniReceptors InterleukinCell BiologyGlycoprotein 130Receptors Interleukin-6Fusion proteinbiological factorsCell biologyOligodeoxyribonucleotidesInterleukin-6 receptorCancer researchSignal transductionCytokine receptorProtein BindingSignal TransductionFEBS Letters
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