Search results for "Protein structure"

showing 10 items of 757 documents

Topology-Dependent Swichability of Peptide Secondary Structures in Bioconjugates with Complex Architectures

2013

Peptide sequences, which exhibit a reversible pH-responsive coil to α-helix secondary structure transition, are conjugated to polymer precursors to yield linear AB and graft ABA peptide-poly(ethylene oxide) conjugates. While the PEO B-block is comparable, the conjugates differ in topologies of the peptide bearing A-blocks. The influences of topology on the structure transitions in the peptide segments are investigated, comparing linear AB-bioconjugates with graft ABA-bioconjugates having multiple peptide segments combined in star or pom-pom topologies.

chemistry.chemical_classificationPolymers and PlasticsEthylene oxideOrganic ChemistryPeptidePolymerConjugated systemMicroscopy Atomic ForceTopologyCombinatorial chemistryProtein Structure SecondaryPolyethylene Glycolschemistry.chemical_compoundchemistryMaterials ChemistrySelf-assemblyPeptidesProtein secondary structureTopology (chemistry)ConjugateMacromolecular Rapid Communications
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Acetylcholine esterase: the structure.

1991

chemistry.chemical_classificationbiologyMolecular StructureSpatial structureProtein ConformationActive siteBiochemistryAcetylcholinesteraseAcetylcholine esterasechemistry.chemical_compoundEnzymeProtein structurechemistryBiochemistrybiology.proteinAcetylcholinesteraseMolecular BiologyTrends in biochemical sciences
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ElaC Encodes a Novel Binuclear Zinc Phosphodiesterase

2002

ElaC is a widespread gene found in eubacteria, archaebacteria, and mammals with a highly conserved sequence. Two human ElaC variants were recently associated with cancer (Tavtigian, S. V., Simard, J., Teng, D. H., Abtin, V., Baumgard, M., Beck, A., Camp, N. J., Carillo, A. R., Chen, Y., Dayananth, P., Desrochers, M., Dumont, M., Farnham, J. M., Frank, D., Frye, C., Ghaffari, S., Gupte, J. S., Hu, R., Iliev, D., Janecki, T., Kort, E. N., Laity, K. E., Leavitt, A., Leblanc, G., McArthur-Morrison, J., Pederson, A., Penn, B., Peterson, K. T., Reid, J. E., Richards, S., Schroeder, M., Smith, R., Snyder, S. C., Swedlund, B., Swensen, J., Thomas, A., Tranchant, M., Woodland, A. M., Labrie, F., Sko…

chemistry.chemical_elementZincBiologymedicine.disease_causeBiochemistrybeta-LactamasesHomology (biology)Conserved sequenceGene productEscherichia colimedicineHistidineCloning MolecularBinding siteMolecular BiologyEscherichia coliHistidineCell NucleusIonsBinding SitesModels StatisticalPhosphoric Diester HydrolasesSpectrum AnalysisX-RaysPhosphodiesteraseCell BiologyProtein Structure TertiaryOxygenKineticsZincBiochemistrychemistryChromatography GelProtonsDimerizationProtein BindingJournal of Biological Chemistry
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Conformational investigation of α,β‐dehydropeptides Part VI. Molecular and crystal structure of benzyloxycarbonylglycyl‐(Z )‐dehydrophenylalanine

1994

The structure of a peptide containing C-terminal dehydrophenylalanine, Z-Gly-(Z)-delta Phe (C19H18N2O5, MW = 354) was determined from single-crystal X-ray diffraction data. Needle-shaped crystals were grown from a 1:1 mixture of methanol-acetone in the monoclinic space group P2(1) with a = 14.717(4), b = 4.941(2), c = 12.073(4) A, beta = 103.72(4) degrees; V = 852.86(8) A3, Z = 2 and Dc = 1.32 g cm-3. The structure was solved by direct methods using SHELXS-86 and refined to a final R-index of 0.032 for 1714 observed reflections. The peptide adopts a conformation folded at the glycine residue, and principal torsion angles are omega 0 = -167.6(2) degrees, phi 1 = -71.8(3) degrees, psi 1 = -31…

conformationdehydropeptidehydrogen bondProtein ConformationChemistryHydrogen bondhelical conformersIntermolecular forceDipeptidesCrystal structuredehydrophenylalanineBiochemistryZ‐Gly‐(Z )‐APheCrystallographyProtein structureX-Ray DiffractionIntramolecular forceSpectroscopy Fourier Transform InfraredX-ray crystallographyMoleculeinfrared spectroscopyX‐ray structure analysisMonoclinic crystal systemInternational Journal of Peptide and Protein Research
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Receptor for advanced glycation end products is subjected to protein ectodomain shedding by metalloproteinases.

2008

The receptor for advanced glycation end products (RAGE) is a 55-kDa type I membrane glycoprotein of the immunoglobulin superfamily. Ligand-induced up-regulation of RAGE is involved in various pathophysiological processes, including late diabetic complications and Alzheimer disease. Application of recombinant soluble RAGE has been shown to block RAGE-mediated pathophysiological conditions. After expression of full-length RAGE in HEK cells we identified a 48-kDa soluble RAGE form (sRAGE) in the culture medium. This variant of RAGE is smaller than a 51-kDa soluble version derived from alternative splicing. The release of sRAGE can be induced by the phorbol ester PMA and the calcium ionophore c…

endocrine system diseasesADAM10Receptor for Advanced Glycation End ProductsMatrix Metalloproteinase InhibitorsHydroxamic AcidsBiochemistryProtein biotinylationCell LineDiabetes ComplicationsADAM10 ProteinGlycationAlzheimer DiseaseHumansProtein IsoformsProtease Inhibitorscardiovascular diseasesRNA Small InterferingReceptors ImmunologicReceptorMolecular BiologyProtein kinase CCalcimycinIonophoresChemistryHEK 293 cellsCell Membranenutritional and metabolic diseasesMembrane ProteinsCell BiologyProtein Structure TertiaryADAM ProteinsAlternative SplicingEctodomainBiochemistryMatrix Metalloproteinase 9cardiovascular systemCarcinogensImmunoglobulin superfamilyTetradecanoylphorbol AcetateAmyloid Precursor Protein Secretaseshuman activitiesThe Journal of biological chemistry
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Higher plants possess two different types of ATX1-like copper chaperones.

2007

Abstract Copper (Cu) chaperones constitute a family of small Cu+-binding proteins required for Cu homeostasis in eukaryotes. The ATX1 family of Cu chaperones specifically delivers Cu to heavy metal P-type ATPases. The plant Arabidopsis thaliana expresses the ATX1-like Cu chaperone CCH, which exhibits a plant-specific carboxy-terminal domain (CTD) with unique structural properties. We show that CCH homologues from other higher plants contain CTDs with structural properties similar to Arabidopsis CCH. Furthermore, we identify a new ATX1-like Cu chaperone in Arabidopsis, AtATX1, which functionally complements yeast atx1Δ and sod1Δ associated phenotypes, and localizes to the cytosol of Arabidop…

endocrine systemATPaseTwo-hybrid screeningBiophysicsArabidopsischemistry.chemical_elementBiochemistryArabidopsisMolecular BiologyAdenosine TriphosphatasesbiologyArabidopsis ProteinsCell BiologyHistone-Lysine N-Methyltransferasebiology.organism_classificationPhenotypeCopperYeastProtein Structure TertiaryCytosolBiochemistrychemistryChaperone (protein)biology.proteinCopperGenome PlantMolecular ChaperonesTranscription FactorsBiochemical and biophysical research communications
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Type II keratin cDNAs from the rainbow trout: implications for keratin evolution.

2002

From a teleost fish, the rainbow trout Oncorhynchus mykiss, we have cloned and sequenced cDNAs encoding five different type II keratins. The corresponding protein spots, as separated by 2D-PAGE of trout cytoskeletal preparations, have been identified by peptide mass mapping using MALDI mass spectrometry. Three of the sequenced keratins are expressed in the epidermis (subtype IIe), and two in simple epithelia and mesenchymal cells (subtype IIs). The IIs keratins are both orthologs of human K8. This leaves unsequenced only the trace component S3 of the biochemically established trout keratin catalog. A phylogenetic tree has been constructed from a multiple alignment of the rod domains of the …

endocrine systemCancer Researchanimal structuresDNA ComplementaryMolecular Sequence Datamacromolecular substancesPeptide MappingType II keratinEvolution MolecularMesodermSpecies SpecificityAntibody SpecificityKeratinAnimalsHumansProtein IsoformsAmino Acid SequenceCloning MolecularMolecular BiologyZebrafishPhylogenyZebrafishchemistry.chemical_classificationGeneticsMammalsMultiple sequence alignmentintegumentary systembiologyPhylogenetic treeSequence Homology Amino AcidLampreyAntibodies MonoclonalLampreysEpithelial CellsCell Biologybiology.organism_classificationProtein Structure TertiaryTroutchemistryOrgan SpecificityOncorhynchus mykissSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationSharksKeratinsRainbow troutEpidermisSequence AlignmentDevelopmental BiologyDifferentiation; research in biological diversity
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2004

Background Arabidopsis thaliana copper metallochaperone CCH is a functional homologue of yeast antioxidant ATX1, involved in cytosolic copper transport. In higher plants, CCH has to be transported to specialised cells through plasmodesmata, being the only metallochaperone reported to date that leaves the cell where it is synthesised. CCH has two different domains, the N-terminal domain conserved among other copper-metallochaperones and a C-terminal domain absent in all the identified non-plant metallochaperones. The aim of the present study was the biochemical and biophysical characterisation of the C-terminal domain of the copper metallochaperone CCH.

endocrine systembiologyfood and beverageschemistry.chemical_elementPlasmodesmabiology.organism_classificationCopperYeastMetallochaperonesCytosolProtein structurechemistryBiochemistryStructural BiologyArabidopsisBiophysicsPeptide sequenceBMC Structural Biology
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Membrane Protein Complexes: Structure and Function

2018

This edited book contains a compilation of 14 advanced academic chapters dealing with the structure and function of membrane protein complexes. This rapidly advancing important field of study closely parallels those on soluble protein complexes, and viral protein and nucleoprotein complexes.Diverse topics are included in this book, ranging from membrane–bound enzymes to ion channels, proton pumps and photosystems. Data from X-ray crystallography, cryo-electron microscopy and other biophysical and biochemical techniques are presented throughout the book. There is extensive use of colour figures of protein structures. Throughout the book structure and function are closely correlated.The two e…

functionprotein complexesViral proteineducationComputational biologyBiologymedicine.disease_causehumanitiesStructure and functionProtein structureMembrane proteinMembrane proteinsmedicinestructure
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The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS

2007

Membrane fission is an essential process in membrane trafficking and other cellular functions. While many fissioning and trafficking steps are mediated by the large GTPase dynamin, some fission events are dynamin independent and involve C-terminal-binding protein-1/brefeldinA-ADP ribosylated substrate (CtBP1/BARS). To gain an insight into the molecular mechanisms of CtBP1/BARS in fission, we have studied the role of this protein in macropinocytosis, a dynamin-independent endocytic pathway that can be synchronously activated by growth factors. Here, we show that upon activation of the epidermal growth factor receptor, CtBP1/BARS is (a) translocated to the macropinocytic cup and its surroundi…

genetic structuresEndocytic cycleGTPaseBiologyTRANSCRIPTIONAL COREPRESSOREPIDERMAL GROWTH-FACTORArticleGeneral Biochemistry Genetics and Molecular BiologySYNAPTIC VESICLE ENDOCYTOSISMembrane fissionCell Line TumorMacropinocytic cupHumansPhosphorylationMacropinosomeMolecular BiologyDynaminEpidermal Growth FactorGeneral Immunology and MicrobiologyMEMBRANE FISSIONGeneral NeuroscienceActinsEnterovirus B HumanProtein Structure TertiaryTransport proteinCell biologyDNA-Binding ProteinsAlcohol OxidoreductasesProtein Transportp21-Activated KinasesPLASMA-MEMBRANEPinocytosisPhosphorylationCell Surface ExtensionsIntegrin alpha2beta1The EMBO Journal
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