Search results for "conformation"

showing 10 items of 1414 documents

HPLC demonstration that an all Trp--Phe replacement in gramicidin A results in a conformational rearrangement from beta-helical monomer to double-str…

1995

We have taken advantage of our previously reported high performance liquid chromatographic (HPLC) strategy to investigate the conformational behavior of the optically reversed gramicidin M (gM-), an analog of gramicidin A with all tryptophans replaced by phenylalanines, in different model membranes. It is quantitatively demonstrated for the first time that once inserted in the lipid environment, gM- (unlike the native peptide) undergoes a conformational transition from beta-helical monomers to thermodynamically stable double-stranded dimers. This transition is faster the higher the incubation temperature and can be neatly observed in both small unilamellar phospholipid vesicles and lysophos…

Protein ConformationDimerPhenylalanineBiophysicsPeptideBiochemistryMicelleHigh-performance liquid chromatographyIon ChannelsProtein Structure Secondarychemistry.chemical_compoundStructure-Activity RelationshipGramicidin AOrganic chemistryMolecular BiologyChromatography High Pressure Liquidchemistry.chemical_classificationChemistrytechnology industry and agricultureGramicidinTryptophanMembrane ProteinsMembranes ArtificialCell BiologyCrystallographyMembraneMonomerlipids (amino acids peptides and proteins)Double strandedBiochemical and biophysical research communications
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Sequence Determines Degree of Knottedness in a Coarse-Grained Protein Model

2015

Knots are abundant in globular homopolymers but rare in globular proteins. To shed new light on this long-standing conundrum, we study the influence of sequence on the formation of knots in proteins under native conditions within the framework of the hydrophobic-polar (HP) lattice protein model. By employing large scale Wang-Landau simulations combined with suitable Monte Carlo trial moves we show that, even though knots are still abundant on average, sequence introduces large variability in the degree of self-entanglements. Moreover, we are able to design sequences which are either almost always or almost never knotted. Our findings serve as proof of concept that the introduction of just o…

Protein ConformationFOS: Physical sciencesGeneral Physics and AstronomyCondensed Matter - Soft Condensed Matterstomatognathic systemComputer SimulationMathematicsSequence (medicine)chemistry.chemical_classificationQuantitative Biology::BiomoleculesDegree (graph theory)Proteinsfood and beveragesBiomolecules (q-bio.BM)Knot theoryAmino acidsurgical procedures operativeModels ChemicalQuantitative Biology - BiomoleculeschemistryFOS: Biological sciencesProtein modelSoft Condensed Matter (cond-mat.soft)Biological systemHydrophobic and Hydrophilic InteractionsMonte Carlo MethodPhysical Review Letters
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Yeast expression of the cytokine receptor domain of the soluble interleukin-6 receptor

1996

Abstract The complex of the soluble interleukin-6 receptor (sIL-6R) and IL-6 (IL-6) is a potent agonist on cells expressing the signal transducing protein gp130. In contrast, IL-6 alone only stimulates cells which express a membrane bound form of the IL-6R and gp130. The natural occurring sIL-6R is generated by shedding of the membrane receptor and to a lesser extend by alternative splicing. We have inserted the coding sequence of the 323 amino acid residues of the human sIL-6R into an expression/secretion vector suitable for the methylotrophic yeast Pichia pastoris . We obtained, however, no detectable expression and secretion of the recombinant protein. When we used only the coding sequen…

Protein ConformationGenetic VectorsImmunologyReceptors InterleukinInterleukin-17 receptorBiologyGlycoprotein 130biology.organism_classificationReceptors Interleukin-6Molecular biologyPichiaPichia pastorisSolubilityAntigens CDInterleukin-4 receptorInterleukin-21 receptorImmunology and Allergy5-HT5A receptorReceptors CytokineCytokine receptorCommon gamma chainJournal of Immunological Methods
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Bishistidyl heme hexacoordination, a key structural property in Drosophila melanogaster hemoglobin

2005

Hemoglobins at high concentration have been isolated long ago from some insect larvae living in hypoxic environments. Conversely, a monomeric hemoglobin has been discovered recently in the fruit fly Drosophila melanogaster as intracellular protein expressed both in larvae and in the adult fly. Such a finding indicates that the oxygen supply in insects may be more complex than previously thought, relying not only on O2 diffusion through the tubular tracheal system, but also on carrier-mediated transport and storage. We present here the crystal structure of recombinant D. melanogaster hemoglobin at 1.20 A resolution. Spectroscopic data show that the protein displays a hexacoordinated heme, wh…

Protein ConformationHemeMatrix (biology)BiologyCrystallography X-RayLigandsBiochemistrylaw.inventionchemistry.chemical_compoundHemoglobinslawMelanogasterAnimalsDrosophila ProteinsHistidineMolecular BiologyHemeCyclohexylaminesBinding SitesSpectrum AnalysisfungiCell BiologyHEXAbiology.organism_classificationOxygenMyoglobinchemistryBiochemistryAlkanesulfonic AcidsBiophysicsRecombinant DNAHemoglobinDrosophila melanogaster
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Valence Topological Charge-Transfer Indices for Dipole Moments

2003

Valence topological charge-transfer (CT) indices are applied to the calculation of dipole moments. The dipole moments calculated by algebraic and vector semisums of the CT indices are defined. The combination of the CT indices allows the estimation of the dipole moments. The model is generalized for molecules with heteroatoms. The ability of the indices for the description of the molecular charge distribution is established by comparing them with the dipole moment of the valence-isoelectronic series of benzene and styrene. Two CT indices, μ v e c (vector semisum of vertex-pair dipole moments) and μ V v e c (valence μ v e c ) are proposed. μ v e c and μ V v e c are important for the predicti…

Protein ConformationHeteroatomPharmaceutical ScienceBiochemistryAnalytical ChemistryElectricityComputational chemistryDrug DiscoveryPhysicsvalence topological charge-transfer indexChemistryCharge densityGeneral Medicinemolecular charge distributionCondensed Matter Physicstransdermal drug deliveryChemistry (miscellaneous)Molecular MedicineAtomic physicsInformation SystemsSteric effectsBond dipole momentStatic ElectricityTransition dipole momentBiophysicsElectronsFractal dimensionMolecular physicsBiophysical PhenomenaArticleCatalysislcsh:QD241-441Inorganic Chemistrylcsh:Organic chemistryAtomic orbitalMoleculePhysical and Theoretical ChemistryMolecular BiologyStyreneTopological quantum numberDipole momentModels StatisticalValence (chemistry)Chemical polarityOrganic ChemistryBenzeneModels Theoreticalvalence topological chargetransfer indexElectric dipole momentDipolephenyl alcoholModels ChemicalMoment (physics)Electric dipole transitionMolecules
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The impact of high hydrostatic pressure on structure and dynamics of beta-lactoglobulin

2013

Abstract Methods Combining small-angle X-ray and neutron scattering measurements with inelastic neutron scattering experiments, we investigated the impact of high hydrostatic pressure on the structure and dynamics of β-lactoglobulin (βLG) in aqueous solution. Background βLG is a relatively small protein, which is predominantly dimeric in physiological conditions, but dissociates to monomer below about pH 3. Results High-pressure structural results show that the dimer–monomer equilibrium, as well as the protein–protein interactions, are only slightly perturbed by pressure, and βLG unfolding is observed above a threshold value of 3000 bar. In the same range of pressure, dynamical results put …

Protein ConformationHydrostatic pressureBiophysics02 engineering and technologyLactoglobulinsProtein dynamicsNeutron scatteringNeutron scattering010402 general chemistry01 natural sciencesBiochemistryInelastic neutron scatteringchemistry.chemical_compound[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein foldingMolecular BiologyHydrostatic pressureQuantitative Biology::BiomoleculesAqueous solutionSmall angle X-ray and neutron scatteringProtein dynamics021001 nanoscience & nanotechnology0104 chemical sciencesCrystallographyMonomerchemistryChemical physicsCompressibilityProtein folding0210 nano-technology
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Axolotl MHC architecture and polymorphism.

1999

The MHC of the urodele amphibian Ambystoma mexicanum consists of multiple polymorphic class I loci linked, so far as yet known, to a single class II B locus. This architecture is very different from that of the anuran amphibian Xenopus. The number of class I loci in the axolotl can vary from 6 to 21 according to the haplotypes as shown by cDNA analysis and Southern blot studies in families. These loci can be classified into seven sequence groups with features ranging from the class Ia to the class Ib type. All individuals express genes from at least three of the seven groups, and all individuals possess the class Ia-like type.

Protein ConformationImmunologyGenes MHC Class IIMolecular Sequence DataGenes MHC Class IMajor histocompatibility complexAmbystomaEvolution MolecularMajor Histocompatibility ComplexAxolotlPolymorphism (computer science)Complementary DNAHLA-A2 AntigenImmunology and AllergyAnimalsHumansAmino Acid SequenceAmbystoma mexicanumGeneConserved SequenceSouthern blotGeneticsPolymorphism GeneticbiologyHaplotypebiology.organism_classificationBlotting Southernbiology.proteinEuropean journal of immunology
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Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational…

2003

The large L envelope protein of the hepatitis B virus utilizes a new folding pathway to acquire a dual transmembrane topology in the endoplasmic reticulum (ER). The process involves cotranslational membrane integration and subsequent posttranslational translocation of its preS subdomain into the ER. Here, we demonstrate that the conformational and functional heterogeneity of L depends on the action of molecular chaperones. Using coimmunoprecipitation, we observed specific interactions between L and the cytosolic Hsc70, in conjunction with Hsp40, and between L and the ER-resident BiP in mammalian cells. Complex formation between L and Hsc70 was abolished when preS translocation was artifici…

Protein ConformationImmunoprecipitationHSC70 Heat-Shock Proteinsmacromolecular substancesTopologyProtein structureViral Envelope ProteinsAnimalsHSP70 Heat-Shock ProteinsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsMultidisciplinarybiologyEndoplasmic reticulumHSC70 Heat-Shock ProteinsBiological SciencesPrecipitin TestsTransport proteinProtein TransportMembrane topologyChaperone (protein)COS Cellsbiology.proteinProtein topologyCarrier ProteinsProtein Processing Post-TranslationalMolecular ChaperonesProceedings of the National Academy of Sciences
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Aggregation Kinetics of Bovine Serum Albumin Studied by FTIR Spectroscopy and Light Scattering

2003

To investigate which type of structural and conformational changes is involved in the aggregation processes of bovine serum albumin (BSA), we have performed thermal aggregation kinetics in D(2)O solutions of this protein. The tertiary conformational changes are followed by Amide II band, the secondary structural changes and the formation of beta-aggregates by the Amide I' band and, finally, the hydrodynamic radius of aggregates by dynamic light scattering. The results show, as a function of pD, that: tertiary conformational changes are more rapid as pD increases; the aggregation proceeds through formation of ordered aggregates (oligomers) at pD far from the isoelectric point of the protein;…

Protein ConformationKineticsBiophysicsProtein aggregationBiochemistryProtein Structure SecondaryProtein structureDynamic light scatteringSpectroscopy Fourier Transform InfraredAnimalsScattering RadiationStatic light scatteringDeuterium OxideBovine serum albuminInfrared spectroscopyStatic light scatteringbiologyChemistryOrganic ChemistryTemperatureSerum Albumin BovineConformational changeRandom coilProtein tertiary structureKineticsCrystallographyBovine serum albuminbiology.proteinDynamic light scatteringCattleProtein aggregation
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PLA2-mediated catalytic activation of its inhibitor 25-acetyl-petrosaspongiolide M: serendipitous identification of a new PLA2 suicide inhibitor.

2004

Abstract25-Acetyl-petrosaspongiolide M (PMAc) (1), a mild non-covalent PLA2 inhibitor, unexpectedly recovers, after incubation with bvPLA2, the ability to covalently modify the enzyme target. This study demonstrates the catalytic effect of bvPLA2 in converting 1 in its deacetylated congener petrosaspongiolide M (PM) (2), a strong covalent PLA2 inhibitor whose molecular mechanism of inhibition has already been clarified. Moreover, our findings outline the potential role of PMAc as anti-inflammatory pro-drug, by virtue of its ability of delivering the active PM agent at the site of inflammation, functioning as a suicide inhibitor.

Protein ConformationMarine natural productLigandsBiochemistryMass SpectrometryProtein Structure SecondaryCIRCULAR-DICHROISMchemistry.chemical_compoundProtein structureStructural BiologyBINDINGEnzyme InhibitorsChromatography High Pressure Liquidchemistry.chemical_classificationbiologyMolecular StructureChemistryCircular DichroismHydrolysisTemperatureAcetylationHydrogen-Ion ConcentrationBEE VENOM PHOSPHOLIPASE-A2PoriferaPETROSASPONGIOLIDES M-RBiochemistryCovalent bondINACTIVATIONMANOALIDESpectrometry Mass Electrospray IonizationCYTOSOLIC PHOSPHOLIPASE A(2); BEE VENOM PHOSPHOLIPASE-A2; FLUORESCENCE DISPLACEMENT ASSAY; PETROSASPONGIOLIDES M-R; CIRCULAR-DICHROISM; NATURAL-PRODUCTS; INACTIVATION; MANOALIDE; POTENT; BINDINGStereochemistryBiophysicsGroup II Phospholipases A2CatalysisPhospholipases AAnti-inflammatory compoundManoalidePhospholipase A2NATURAL-PRODUCTSGeneticsTrifluoroacetic acidAnimalsBinding siteOleanolic AcidMolecular BiologyBinding SitesPOTENTCYTOSOLIC PHOSPHOLIPASE A(2)Cell BiologyMolecular WeightKineticsPhospholipases A2EnzymeAcetylationbiology.proteinFLUORESCENCE DISPLACEMENT ASSAYPhospholipase A2 inhibitionFEBS letters
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