Search results for "Protein Structure"

showing 10 items of 757 documents

Amino acid substitutions enhancing thermostability of Bacillus polymyxa beta-glucosidase A

1996

Mutations enhancing the thermostability of β-glucosidase A of Bacillus polymyxa, a family 1 glycosyl hydrolase, have been obtained after hydroxylamine mutagenesis of a plasmid containing the bglA gene, transformation of Escherichia coli with the mutagenized plasmid, and identification of transformant colonies that showed β-glucosidase activity after a thermal treatment that inactivated the wild-type enzyme. Two additive mutations have been characterized that cause replacement of glutamate at position 96 by lysine and of methionine at position 416 by isoleucine respectively. The thermoresistant mutant enzymes showed increased resistance to other denaturing agents, such as pH and urea, while …

Hot TemperatureMutantMolecular Sequence DataBacillusHydroxylamineBiologymedicine.disease_causeHydroxylaminesBiochemistryProtein Structure Secondarychemistry.chemical_compoundHydrolaseEnzyme StabilitymedicineEscherichia coliPoint MutationAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliThermostabilitychemistry.chemical_classificationMethionineBase Sequencebeta-GlucosidaseCell BiologyMolecular biologyRecombinant ProteinsAmino acidKineticschemistryBiochemistryOligodeoxyribonucleotidesMutagenesisMutagenesis Site-DirectedThermodynamicsSpectrophotometry UltravioletIsoleucineCysteineResearch Article
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Role of Solvent on Protein-Matrix Coupling in MbCO Embedded in Water-Saccharide Systems: A Fourier Transform Infrared Spectroscopy Study

2006

AbstractEmbedding protein in sugar systems of low water content enables one to investigate the protein dynamic-structure function in matrixes whose rigidity is modulated by varying the content of residual water. Accordingly, studying the dynamics and structure thermal evolution of a protein in sugar systems of different hydration constitutes a tool for disentangling solvent rigidity from temperature effects. Furthermore, studies performed using different sugars may give information on how the detailed composition of the surrounding solvent affects the internal protein dynamics and structural evolution. In this work, we compare Fourier transform infrared spectroscopy measurements (300–20K) o…

Hot TemperatureProtein ConformationBiophysicsLactosechemistry.chemical_compoundProtein structureRaffinosePolysaccharidesSpectroscopy Fourier Transform InfraredCarbohydrate ConformationFourier transform infrared spectroscopySugarSpectroscopyMaltosechemistry.chemical_classificationMyoglobinBiomoleculeProtein dynamicsTrehaloseWaterProteinsTrehaloseSolventCrystallographyGlucosechemistryChemical physicsSolventsMuramidaseBiophysical Journal
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Sponge Bcl-2 homologous protein (BHP2-GC) confers distinct stress resistance to human HEK-293 cells

2001

It is established that sponges, the phylogenetically oldest still extant phylum of Metazoa, possess key molecules of the apoptotic pathways, that is members from the Bcl-2 family and a pro-apoptotic molecule with death domains. Here we report on transfection studies of human cells with a sponge gene, GCBHP2. Sponge tissue was exposed to heat shock and tributyltin, which caused an upregulation of gene expression of GCBHP2. The cDNA GCBHP2 was introduced into human HEK-293 cells and mouse NIH-3T3 cells; the stable transfection was confirmed by the identification of the transcripts, by Western blotting as well as by immunofluorescence using antibodies raised against the recombinant polypeptide…

Hot Temperatureanimal structuresCell SurvivalvirusesMolecular Sequence DataDrug ResistanceApoptosisAntibodiesCell LineMiceComplementary DNAGene expressionAnimalsHumansAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyPhylogenySequence Homology Amino AcidbiologyCaspase 3ChemistryfungiHEK 293 cellsCell BiologyTransfectionbiology.organism_classificationMolecular biologyPoriferaProtein Structure TertiaryUp-RegulationEnzyme ActivationBlotSpongeProto-Oncogene Proteins c-bcl-2Cell cultureCaspasesembryonic structuresbiology.proteinTrialkyltin CompoundsAntibodySequence AlignmentHeat-Shock ResponseCell Death & Differentiation
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Primary Structure of Selected Archaeal Mesophilic and Extremely Thermophilic Outer Surface Layer Proteins

2002

The archaea are recognized as a separate third domain of life together with the bacteria and eucarya. The archaea include the methanogens, extreme halophiles, thermoplasmas, Sulfate reducers and Sulfur metabolizing thermophiles, which thrive in different habitats such as anaerobic niches, salt lakes, and marine hydrothermals systems and continental solfataras. Many of these habitats represent extreme environments in respect to temperature, osmotic pressure and pH-values and remind on the conditions of the early earth. The cell envelope structures were one of the first biochemical characteristics of archaea studied in detail. The most common archaeal cell envelope is composed of a single cry…

Hot TemperaturebiologyArchaeal ProteinsThermophileThermoplasmaMembrane ProteinsProtein Sorting Signalsbiology.organism_classificationArchaeaApplied Microbiology and BiotechnologyMicrobiologyProtein Structure SecondaryHalophileBiochemistryExtreme environmentAmino Acid SequenceAmino AcidsCell envelopeProtein stabilizationSequence AlignmentS-layerEcosystemEcology Evolution Behavior and SystematicsArchaeaSystematic and Applied Microbiology
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Purification, crystallization and preliminary X-ray studies of sylvaticin, an elicitin-like protein from Pythium sylvaticum.

2003

Sylvaticin belongs to the elicitin family. These 10 kDa oomycetous proteins induce a hypersensitive response in plants, including necrosis and cell death, but subsequently leading to a non-specific systemic acquired resistance (SAR) against other pathogens. Sylvaticin has been crystallized using PEG 2000 MME as a precipitant agent in the presence of nickel chloride. The crystals belong to space group C2, with unit-cell parameters a = 99.29, b = 25.67, c = 67.45 A, beta = 99.66 degrees. Diffraction data were recorded to 2.1 A resolution at a synchrotron-radiation source.

Hypersensitive responseStereochemistryProtein ConformationPythiumBiologyCrystallography X-Raylaw.inventionPolyethylene GlycolsProtein structureStructural BiologylawNickelPEG ratioCrystallizationFuransAlgal ProteinsX-rayProteinsElicitinGeneral Medicinebiology.organism_classificationCrystallographySolventsPythium sylvaticumSystemic acquired resistanceSynchrotronsActa crystallographica. Section D, Biological crystallography
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Nouvelles perspectives concernant la structure et la fonction du domaine carboxyl terminal de Hfq

2015

Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to…

IDP intrinsically-disordered proteinslcsh:Lifelcsh:QR1-502sub-membrane macromolecular assemblyPlasma protein bindingsRNA small non-coding RNABiochemistrylcsh:Microbiologyamyloid fibrilsProtein biosynthesis0303 health sciences[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Escherichia coli Proteins030302 biochemistry & molecular biologyHfqCTRp Hfq C-terminal peptideFTIR Fourier transform infrared spectroscopyNTR N-terminal regionCompartmentalization (psychology)Cell biology[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsRNA Bacterialsmall non-coding ribonucleic acid (RNA)BiochemistryFSD Fourier self-deconvolutionTransfer RNAAmyloid fibrilProtein BindingBiophysicsBiologyHost Factor 1 Protein03 medical and health sciencesEscherichia coliThT thioflavin T[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein Structure QuaternaryncRNA regulatory non-coding RNAPost-transcriptional regulationMolecular Biology030304 developmental biologyOriginal PaperC-terminusRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyCell Biologycellular compartmentalizationWT wild-typeProtein Structure Tertiarylcsh:QH501-531Host Factor 1 ProteinCTR Hfq C-terminal regionribonucleic acid (RNA) processing and degradationBiophysicpost-transcriptional regulationBioscience Reports
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Inhibition of the Cysteine Protease Human Cathepsin L by Triazine Nitriles: Amide⋅⋅⋅Heteroarene π-Stacking Interactions and Chalcogen Bonding in the …

2016

We report an extensive "heteroarene scan" of triazine nitrile ligands of the cysteine protease human cathepsin L (hCatL) to investigate π-stacking on the peptide amide bond Gly67-Gly68 at the entrance of the S3 pocket. This heteroarene⋅⋅⋅peptide bond stacking was supported by a co-crystal structure of an imidazopyridine ligand with hCatL. Inhibitory constants (Ki ) are strongly influenced by the diverse nature of the heterocycles and specific interactions with the local environment of the S3 pocket. Binding affinities vary by three orders of magnitude. All heteroaromatic ligands feature enhanced binding by comparison with hydrocarbon analogues. Predicted energetic contributions from the ori…

ImidazopyridineNitrileStereochemistryCathepsin LPeptideMolecular Dynamics Simulation010402 general chemistryCrystallography X-RayLigands01 natural sciencesBiochemistrychemistry.chemical_compoundAmideDrug DiscoveryHydrolaseNitrilesPeptide bondHumansGeneral Pharmacology Toxicology and PharmaceuticsTriazinePharmacologychemistry.chemical_classificationBinding Sites010405 organic chemistryChemistryLigandTriazinesOrganic ChemistryAmides0104 chemical sciencesProtein Structure TertiaryMolecular MedicineChalcogensQuantum TheoryProtein BindingChemMedChem
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AML-associated Flt3 kinase domain mutations show signal transduction differences compared with Flt3 ITD mutations

2005

Activating mutations of Flt3 are found in approximately one third of patients with acute myeloid leukemia (AML) and are an attractive drug target. Two classes of Flt3 mutations occur: internal tandem duplications (ITDs) in the juxtamembrane and point mutations in the tyrosine kinase domain (TKD). We and others have shown that Flt3-ITD induced aberrant signaling including strong activation of signal transducer and activator of transcription 5 (STAT5) and repression of CCAAT/estradiol-binding protein α (c/EBPα) and Pu.1. Here, we compared the signaling properties of Flt3-ITD versus Flt3-TKD in myeloid progenitor cells. We demonstrate that Flt3-TKD mutations induced autonomous growth of 32D ce…

ImmunologyApoptosisBiologymedicine.disease_causeBiochemistryCell Linefluids and secretionsProto-Oncogene Proteinshemic and lymphatic diseasesSTAT5 Transcription FactormedicineAnimalsHumansPoint MutationMyeloid CellsPhosphorylationProtein kinase BProtein kinase CMutationPoint mutationAutophosphorylationIntracellular Signaling Peptides and ProteinsReceptor Protein-Tyrosine Kinaseshemic and immune systemsCell BiologyHematologyMilk ProteinsStaurosporineMolecular biologyProtein Structure TertiaryDNA-Binding ProteinsMuridaefms-Like Tyrosine Kinase 3Leukemia MyeloidTandem Repeat SequencesAcute Diseaseembryonic structuresFms-Like Tyrosine Kinase 3Mutagenesis Site-DirectedTrans-ActivatorsSignal transductionTyrosine kinaseSignal TransductionTranscription FactorsBlood
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Relationship between within-host fitness and virulence in the vesicular stomatitis virus: correlation with partial decoupling.

2012

ABSTRACT Given the parasitic nature of viruses, it is sometimes assumed that rates of viral replication and dissemination within hosts (within-host fitness) correlate with virulence. However, there is currently little empirical evidence supporting this principle. To test this, we quantified the fitness and virulence of 21 single- or double-nucleotide mutants of the vesicular stomatitis virus in baby hamster kidney cells (BHK-21). We found that, overall, these two traits correlated positively, but significant outliers were identified. Particularly, a single mutation in the conserved C terminus of the N nucleocapsid (U1323A) had a strongly deleterious fitness effect but did not alter or even …

ImmunologyMutantVirulenceApoptosisBiologymedicine.disease_causeVirus ReplicationMicrobiologyVesicular stomatitis Indiana virusCell Line03 medical and health sciencesVesicular StomatitisMiceVirologyCricetinaemedicineBaby hamster kidney cellAnimals030304 developmental biologyGlycoproteinsGenetics0303 health sciencesMutationMice Inbred BALB CVirulence030302 biochemistry & molecular biologyCell MembraneBrainNucleocapsid Proteinsbiology.organism_classification3. Good healthProtein Structure TertiaryViral replicationGenetic Diversity and EvolutionVesicular stomatitis virusInsect ScienceMutationFemaleNeuron deathVesicular StomatitisJournal of virology
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Human Siglec-10 can bind to vascular adhesion protein-1 and serves as its substrate

2009

AbstractLeukocytes migrate from the blood into areas of inflammation by interacting with various adhesion molecules on endothelial cells. Vascular adhesion protein-1 (VAP-1) is a glycoprotein expressed on inflamed endothelium where it plays a dual role: it is both an enzyme that oxidizes primary amines and an adhesin that is involved in leukocyte trafficking to sites of inflammation. Although VAP-1 was identified more than 15 years ago, the counterreceptor(s) for VAP-1 on leukocytes has remained unknown. Here we have identified Siglec-10 as a leukocyte ligand for VAP-1 using phage display screenings. The binding between Siglec-10 and VAP-1 was verified by different adhesion assays, and this…

ImmunologyReceptors Cell SurfaceInflammationCHO CellsPlasma protein bindingBiologyLigandsBiochemistryMice03 medical and health sciencesCricetulus0302 clinical medicinePeptide LibraryVascular BiologyCricetinaeLectinsLeukocyte TraffickingCell AdhesionmedicineAnimalsHumansEndotheliumLymphocytesProtein Structure QuaternaryCell adhesion030304 developmental biologyMice Knockout0303 health sciencesCell adhesion moleculeSoluble cell adhesion moleculesSIGLECCell BiologyHematologyAdhesionrespiratory systembacterial infections and mycosesRecombinant Proteinsrespiratory tract diseasesChemotaxis LeukocyteBiochemistry030220 oncology & carcinogenesisAmine Oxidase (Copper-Containing)medicine.symptomCell Adhesion MoleculesProtein BindingBlood
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