Search results for "Protein Structure"

showing 10 items of 757 documents

(Strept)avidin as host for biotinylated coordination complexes: stability, chiral discrimination, and cooperativity

2005

Incorporation of a biotinylated ruthenium tris(bipyridine) [Ru(bpy)₂(Biot-bpy)]²⁺ (1) in either avidin or streptavidin-(strept)avidin-can be conveniently followed by circular dichroism spectroscopy. To determine the stepwise association constants, cooperativity, and chiral discrimination properties, diastereopure (Λ and δ)-1 species were synthesized and incorporated in tetrameric (strept)avidin to afford (δ-[Ru(bpy)₂(Biot-bpy)]²⁺)x⊂avidin, (Λ- [Ru(bpy)₂(Biot-bpy)]²⁺)x⊂avidin, (δ-[Ru(bpy)₂(Biot- bpy)]²⁺)x⊂streptavidin, and (Λ-[Ru(bpy)₂(Biot-bpy)]²⁺) x⊂streptavidin (x = 1-4) For these four systems, the overall stability constants are log β₄ = 28.6, 30.3, 36.2, and 36.4, respectively. Critical…

StreptavidinCircular dichroismProtein ConformationStereochemistryBiotinchemistry.chemical_elementCooperativity010402 general chemistry01 natural sciencesInorganic ChemistryStructure-Activity RelationshipBipyridinechemistry.chemical_compound22'-DipyridylBacterial ProteinsBiotinCoordination ComplexesBiotinylation[CHIM.COOR]Chemical Sciences/Coordination chemistryPhysical and Theoretical ChemistryComputingMilieux_MISCELLANEOUSMolecular Structurebiology010405 organic chemistry[ CHIM.COOR ] Chemical Sciences/Coordination chemistryAvidinProtein Structure Tertiary0104 chemical sciencesRuthenium[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryCrystallographychemistryBiotinylation[ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistrybiology.proteinStreptavidinAvidin
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X-ray diffraction of a protein crystal anchored at the air/water interface

1995

We report the first successful in situ x-ray diffraction experiment with a 2D protein array at the lipid/water interface and demonstrate that the order can be controlled via lateral pressure or density. A protein (streptavidin) was bound to a monolayer of biotinylated lipid at the air/water interface, and diffraction of the protein layer could be measured to many orders. Compression of the monolayer changed the diffraction pattern drastically, indicating that the protein structure can be strongly influenced by external parameters like lateral pressure or density. From the width of the peaks, we find that aggregates consisting of as few as 100 monomers contribute to the diffraction. This ind…

StreptavidinDiffractionProtein ConformationAnalytical chemistryBiophysicsCrystallography X-RayBiophysical Phenomenalaw.inventionCrystalchemistry.chemical_compoundProtein structureBacterial ProteinslawMonolayerCrystallizationPhospholipidsGrazing incidence diffractionMolecular StructureAirfood and beveragesProteinsWaterCrystallographychemistryX-ray crystallographyStreptavidinResearch ArticleBiophysical Journal
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Recombinant NeutraLite Avidin: a non-glycosylated, acidic mutant of chicken avidin that exhibits high affinity for biotin and low non-specific bindin…

2000

AbstractA recombinant non-glycosylated and acidic form of avidin was designed and expressed in soluble form in baculovirus-infected insect cells. The mutations were based on the same principles that guided the design of the chemically and enzymatically modified avidin derivative, known as NeutraLite Avidin. In this novel recombinant avidin derivative, five out of the eight arginine residues were replaced with neutral amino acids, and two of the lysine residues were replaced by glutamic acid. In addition, the carbohydrate-bearing asparagine-17 residue was altered to an isoleucine, according to the known sequences of avidin-related genes. The resultant mutant protein, termed recombinant Neutr…

StreptavidinGlycosylationMolecular Sequence DataBiophysicsBiotinChick EmbryoNon-specific bindingBiochemistrylaw.inventionchemistry.chemical_compoundBiotinstomatognathic systemStructural BiologylawMutant proteinNon-glycosylated mutantGeneticsAnimalsHumansAmino Acid SequenceIsoelectric PointProtein Structure QuaternaryMolecular BiologyCells CulturedbiologyAvidin-biotin technologyDNACell BiologyProtein engineeringrespiratory systemAvidinRecombinant ProteinsKineticsAmino Acid SubstitutionchemistryBiochemistryBiotinylationMutationbiology.proteinRecombinant DNAThermodynamicsProtein engineeringEndopeptidase KIsoleucineBaculoviridaeProtein BindingAvidinFEBS Letters
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Dimer-tetramer transition between solution and crystalline states of streptavidin and avidin mutants.

2003

ABSTRACT The biotin-binding tetrameric proteins, streptavidin from Streptomyces avidinii and chicken egg white avidin, are excellent models for the study of subunit-subunit interactions of a multimeric protein. Efforts are thus being made to prepare mutated forms of streptavidin and avidin, which would form monomers or dimers, in order to examine their effect on quaternary structure and assembly. In the present communication, we compared the crystal structures of binding site W→K mutations in streptavidin and avidin. In solution, both mutant proteins are known to form dimers, but upon crystallization, both formed tetramers with the same parameters as the native proteins. All of the intersub…

StreptavidinModels MolecularStereochemistryProtein ConformationDimerBiotinCrystallography X-RayMicrobiologychemistry.chemical_compoundProtein structureBiotinTetramerEgg WhiteStructural BiologyAnimalsProtein Structure QuaternaryMolecular BiologyBinding SitesbiologyAvidinStreptomycesSolutionschemistryBiochemistryBiotinylationMutationbiology.proteinProtein quaternary structureStreptavidinCarrier ProteinsCrystallizationChickensDimerizationAvidinJournal of bacteriology
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Crystallization and preliminary X-ray analysis of W120K mutant of streptavidin.

2001

Bacterial streptavidin and chicken avidin are homotetrameric proteins that share an exceptionally high affinity towards the vitamin biotin. The biotin-binding sites in both proteins contain a crucial tryptophan residue contributed from an adjacent subunit. This particular tryptophan (W110 in avidin and W120 in streptavidin) plays an important role in both biotin binding and in the quaternary stabilities of the proteins. An intriguing naturally occurring alteration of tryptophan to lysine was previously described in the C-terminal domain of sea-urchin fibropellins, which share a relatively high sequence similarity with avidin and streptavidin. Avidin (Avm-W110K) and streptavidin (Savm-W120K)…

StreptavidinStrep-tagBiotin bindingbiologyProtein ConformationLysineTryptophanTryptophanGeneral MedicineCrystallography X-Raychemistry.chemical_compoundCrystallographyProtein structureBiotinchemistryAmino Acid SubstitutionBacterial ProteinsStructural BiologyBiotinylationMutationbiology.proteinStreptavidinCrystallizationBaculoviridaeAvidinActa crystallographica. Section D, Biological crystallography
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A comparative study of carboxy myoglobin in saccharide-water systems by molecular dynamics simulation.

2007

Results from room-temperature molecular dynamics simulation on a system containing carboxy-myoglobin, water, and maltose molecules are reported. Protein atomic fluctuations, protein−solvent and solvent−solvent hydrogen bonding have been analyzed and compared to the ones in trehalose−water and sucrose−water systems (Proteins 2005, 59, 291−302). Results help in rationalizing, at a molecular level, the effects of homologues disaccharides on protein structure/dynamics experimentally observed. Furthermore, the effectiveness of disaccharides in bioprotection in terms of peculiar protein−matrix coupling is also discussed.

SucroseHydrogen bondMyoglobinmyoglobin simulation conformational substates disaccharideTrehaloseWaterHydrogen BondingMaltoseSurfaces Coatings and FilmsProtein Structure Tertiarychemistry.chemical_compoundMolecular dynamicsProtein structureMolecular levelchemistryMyoglobinModels ChemicalComputational chemistryMaterials ChemistryMoleculeComputer SimulationPhysical and Theoretical ChemistryMaltoseThe journal of physical chemistry. B
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Thermal Aggregation of Bovine Serum Albumin in Trehalose and Sucrose Aqueous Solutions

2012

We report results of static and dynamic light scattering measurements performed on bovine serum albumin (BSA) in saccharide (trehalose and sucrose) solutions. Our aim is to study the effects of the two disaccharides on the first steps of thermal aggregation of BSA in aqueous solutions at two protein concentrations (1 and 30 mg/mL) at increasing sugar/water ratio. Results show that sugars modify early stages of aggregation mainly by perturbing the thermodynamic behavior of the solvent (i.e., general solvent effects) without involving direct, specific sugar-protein interactions. This agrees with current hypotheses on sugar action in protein solutions. (1-3) The linear correlation detected bet…

SucroseSucrosechemistry.chemical_compoundDynamic light scatteringMaterials ChemistryAnimalsTransition TemperaturePhysical and Theoretical ChemistryBovine serum albuminProtein Structure QuaternarySugarChromatographyAqueous solutionbiologyTemperatureTrehaloseWaterSerum Albumin BovineTrehaloseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Surfaces Coatings and FilmsSolutionsSolventtrehalose protein aggregation solvent effects light scatteringchemistrySolventsbiology.proteinCattleProtein MultimerizationSolvent effectsThe Journal of Physical Chemistry B
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Protein Kinase C-dependent Ubiquitination and Clathrin-mediated Endocytosis of the Cationic Amino Acid Transporter CAT-1*

2011

Cationic amino acid transporter 1 (CAT-1) is responsible for the bulk of the uptake of cationic amino acids in most mammalian cells. Activation of protein kinase C (PKC) leads to down-regulation of the cell surface CAT-1. To examine the mechanisms of PKC-induced down-regulation of CAT-1, a functional mutant of CAT-1 (CAT-1-HA-GFP) was generated in which a hemagglutinin antigen (HA) epitope tag was introduced into the second extracellular loop and GFP was attached to the carboxyl terminus. CAT-1-HA-GFP was stably expressed in porcine aorthic endothelial and human epithelial kidney (HEK) 293 cells. Using the HA antibody internalization assay we have demonstrated that PKC-dependent endocytosis…

Swinemedia_common.quotation_subjectNedd4 Ubiquitin Protein LigasesUbiquitin-Protein LigasesUbiquitin-conjugating enzymeEndocytosisBiochemistryClathrinProtein Structure SecondaryMembrane BiologyAnimalsHumansAmino acid transporterInternalizationMolecular BiologyProtein kinase CProtein Kinase Cmedia_commonCationic Amino Acid Transporter 1biologyEndosomal Sorting Complexes Required for TransportUbiquitinationClathrin-Coated VesiclesCell BiologyReceptor-mediated endocytosisClathrinEndocytosisCell biologyUbiquitin ligaseHEK293 CellsBiochemistrybiology.protein
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Autoimmunity to the p53 protein is a feature of systemic lupus erythematosus (SLE) related to anti-DNA antibodies.

2001

The induction of anti-DNA autoantibodies in systemic lupus erythematosus (SLE) patients is problematic because mammalian DNA is poorly immunogenic at best. Here we demonstrate a chain of connected antibodies in SLE patient sera that could account for the induction of anti-DNA antibody, and possibly for some of the pathogenic features of SLE. We now report that SLE patients, in addition to anti-DNA, produce antibodies to the carboxy-terminal domain of the tumour suppressor molecule p53; this p53 domain recognizes damaged DNA. Hence, these anti-p53 antibodies could mimic damaged DNA immunologically. Indeed, SLE sera do contain anti-idiotypic antibodies to a prototypic anti-p53 antibody. Moreo…

Systemic diseaseAnti-nuclear antibodyImmunologyBiologymedicine.disease_causeProtein Structure SecondaryAutoimmunityImmunoglobulin Idiotypesimmune system diseasesmedicineImmunology and AllergyHumansLupus Erythematosus Systemicskin and connective tissue diseasesAutoantibodiesAutoimmune diseaseLupus erythematosusMolecular MimicryAutoantibodymedicine.diseaseDNA-Binding ProteinsMolecular mimicryAntibodies AntinuclearImmunologyCancer researchbiology.proteinAntibodyTumor Suppressor Protein p53PeptidesJournal of autoimmunity
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Modular organization in the reductive evolution of protein-protein interaction networks

2006

Analysis of the reduction in genome size of Buchnera aphidicola from its common ancestor E. coli shows that the organization of networks into modules is the property that seems to be directly related with the evolutionary process of genome reduction.

Systems biologyComplex systemComputational biologyBiologyGenomeProtein protein interaction networkProtein–protein interactionBuchneraInteraction networkProtein Interaction MappingEscherichia coliAnimalsHumansDatabases ProteinGeneticsbusiness.industrySystems BiologyResearchbiochemical phenomena metabolism and nutritionModular designbiology.organism_classificationBiological EvolutionProtein Structure TertiaryStructural Homology ProteinMultiprotein ComplexesBuchnerabusinessAlgorithmsGenome BacterialGenome Biology
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