Search results for "Protein structure"

showing 10 items of 757 documents

Chemical and physical characterization of thermal aggregation of model proteins modulated by zinc(II) and copper(II) ions

2016

BACKGROUND: Metal ions are implicated in protein aggregation processes of several neurodegenerative pathologies, where the protein deposition occurs, and in the biotechnology field like the food technology where many processes in food manufacturing are based on thermal treatments. OBJECTIVE: The influence of Cu2+ or Zn2+ ions on the thermal aggregation process of Bovine beta-lactoglobulin (BLG) and Bovine Serum Albumin (BSA), two protein models, was studied with the aim of delineating the role of these ions in the protein aggregation kinetics and to clarify the related molecular mechanisms. METHODS: The protein structure changes were monitored by Raman spectroscopy, whereas the aggregate gr…

inorganic chemicals0301 basic medicineMetal ions in aqueous solutionKineticsInorganic chemistryBeta-lactoglobulinchemistry.chemical_elementZincProtein aggregation010402 general chemistry01 natural sciencesBovine Serum Albumin (BSA)Beta-lactoglobulin bovine serum albumin (BSA) copper and zinc ionsRaman spectroscopy dynamic light scatteringMetal03 medical and health sciencesProtein structureDynamic light scatteringcopper and zinc ionRadiology Nuclear Medicine and imagingcopper and zinc ionsBovine serum albuminBeta-lactoglobulin; Bovine Serum Albumin (BSA); copper and zinc ions; Raman spectroscopy; dynamic light scatteringbiologydigestive oral and skin physiologydynamic light scattering0104 chemical sciences030104 developmental biologychemistryvisual_artRaman spectroscopyBiophysicsbiology.proteinvisual_art.visual_art_medium
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Nitrated Fatty Acids Modulate the Physical Properties of Model Membranes and the Structure of Transmembrane Proteins

2017

Nitrated fatty acids (NO2 -FAs) act as anti-inflammatory signal mediators, albeit the molecular mechanisms behind NO2 -FAs' influence on diverse metabolic and signaling pathways in inflamed tissues are essentially elusive. Here, we combine fluorescence measurements with surface-specific sum frequency generation vibrational spectroscopy and coarse-grained computer simulations to demonstrate that NO2 -FAs alter lipid organization by accumulation at the membrane-water interface. As the function of membrane proteins strongly depends on both, protein structure as well as membrane properties, we consecutively follow the structural dynamics of an integral membrane protein in presence of NO2 -FAs. …

inorganic chemicals0301 basic medicineProtein Conformationcomplex mixturesPhase TransitionCatalysisPhysical Phenomena03 medical and health sciences0302 clinical medicineProtein structureJournal ArticleFluorescence Resonance Energy TransferMembrane fluidityComputer SimulationLipid bilayerIntegral membrane proteinNitratesChemistryCircular DichroismCell MembraneFatty AcidsOrganic ChemistryPeripheral membrane proteinMembrane ProteinsGeneral Chemistryrespiratory systemLipidsTransmembrane protein030104 developmental biologyMembraneMembrane proteinBiochemistryBiophysics030217 neurology & neurosurgerySignal TransductionChemistry – A European Journal
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Metal ions modulate thermal aggregation of betalactoglobulin: a join chemical and physical characterization

2014

Abstract Molecular basis of the role played by Cu 2 + and Zn 2 + ions during the thermal aggregation processes of beta-lactoglobulin (BLG) was studied by using a joint application of different techniques. In particular, Raman spectroscopy was very useful in identifying the different effects caused by the two metals at molecular level (i.e. changes in His protonation state, disulfides bridge conformation, and micro-environment of aromatic residues), evidencing the primary importance of the protein charge distribution during the aggregation process. Both metal ions are able to act on this factor and favor the protein aggregation, but Zn 2 + is able to alter the natural conformational state of…

inorganic chemicalsCOPPER AND ZINC IONSMetal ions in aqueous solutionBeta-lactoglobulin; Copper and zinc ions; Raman spectroscopy; Infrared spectroscopy; Dynamic light scatteringBeta-lactoglobulinInfrared spectroscopyProtonationThermal treatmentLactoglobulinsProtein aggregationCopper and zinc ionSpectrum Analysis RamanBiochemistryFOURIER-TRANSFORM INFRARED SPECTROSCOPYProtein Structure SecondarySupramolecular assemblyIonBOVINE BETA-LACTOGLOBULINInorganic ChemistryProtein AggregatesDynamic light scatteringSpectroscopy Fourier Transform InfraredInfrared spectroscopyIonsChemistryTemperatureCrystallographyZincRaman spectroscopyBeta-lactoglobulin; Copper and zinc ions; Dynamic light scattering; Infrared spectroscopy; Raman spectroscopyDYNAMIC LIGHT SCATTERINGCopper
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Modeling of the N-terminal Section and the Lumenal Loop of Trimeric Light Harvesting Complex II (LHCII) by Using EPR

2015

The major light harvesting complex II (LHCII) of green plants plays a key role in the absorption of sunlight, the regulation of photosynthesis, and in preventing photodamage by excess light. The latter two functions are thought to involve the lumenal loop and the N-terminal domain. Their structure and mobility in an aqueous environment are only partially known. Electron paramagnetic resonance (EPR) has been used to measure the structure of these hydrophilic protein domains in detergent-solubilized LHCII. A new technique is introduced to prepare LHCII trimers in which only one monomer is spin-labeled. These heterogeneous trimers allow to measure intra-molecular distances within one LHCII mon…

inorganic chemicalsModels MolecularProtein ConformationProtein domainTrimerContext (language use)complex mixturesBiochemistrylaw.inventionchemistry.chemical_compoundBiopolymersProtein structurelawElectron paramagnetic resonanceMolecular BiologySuperhelixfungiElectron Spin Resonance SpectroscopyPhotosystem II Protein ComplexCell Biologyequipment and suppliesCrystallographyMonomerModels ChemicalchemistryThylakoidProtein Structure and FoldingbacteriaJournal of Biological Chemistry
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FTIR analysis of the high pressure response of native insulin assemblies

2013

It is widely recognized that a central role in conferring stability to the structure of proteins against misfolding and aggregation is played by the formation of oligomers. The case of insulin is prototypical in this respect: in our body it is stored up in stable inactive hexameric assemblies whereas only in its monomeric form it recovers the role of regulating carbohydrate and fat metabolism. In the present paper, exploiting the optimal coupling between FTIR spectroscopy and diamond anvil cell technique, we probe the stability of different insulin oligomeric forms under high pressure, namely over the ranges 0-15 kbar for water solution and 0-80 kbar for dry powder. Results obtained show di…

insulinftirInsulinmedicine.medical_treatmentOrganic Chemistryhigh pressure biophysicsdiamond anvil cel; insulin; ftir; high pressure biophysicsCarbohydrateDiamond anvil cellAnalytical ChemistryDiamond anvil cellInorganic ChemistryCoupling (electronics)chemistry.chemical_compoundCrystallographyProtein structureMonomerchemistryHigh pressureBiophysicsmedicinediamond anvil celHigh pressure biophysicFourier transform infrared spectroscopySpectroscopy
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Virulence factor rtx in Legionella pneumophila, evidence suggesting it is a modular multifunctional protein

2008

Abstract Background The repeats in toxin (Rtx) are an important pathogenicity factor involved in host cells invasion of Legionella pneumophila and other pathogenic bacteria. Its role in escaping the host immune system and cytotoxic activity is well known. Its repeated motives and modularity make Rtx a multifunctional factor in pathogenicity. Results The comparative analysis of rtx gene among 6 strains of L. pneumophila showed modularity in their structures. Among compared genomes, the N-terminal region of the protein presents highly dissimilar repeats with functionally similar domains. On the contrary, the C-terminal region is maintained with a fashionable modular configuration, which gives…

lcsh:QH426-470Virulence Factorslcsh:BiotechnologyBacterial ToxinsVirulencemedicine.disease_causeLegionella pneumophilaVirulence factorLegionella pneumophilaMicrobiologyImmune systemBacterial Proteinslcsh:TP248.13-248.65GeneticsmedicineAnimalsHumansCytotoxic T cellPhylogenyVirulencebiologyToxinHost (biology)Pathogenic bacteriabiology.organism_classificationVirologyProtein Structure Tertiarylcsh:GeneticsGenes BacterialResearch ArticleBiotechnologyBMC Genomics
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The C-terminal antibody binding domain ofCandida albicansmp58 represents a protective epitope during candidiasis

2003

The 58-kDa surface mannoprotein of Candida albicans (mp58) elicits strong antibody responses during infection. Epitope mapping with sera from patients with candidiasis and control individuals indicated the presence of multiple IgG-reactive continuous epitopes on the protein, expanding both the amino- and carboxy-terminal domains and several internal regions. These immunoreactive regions were similar to the ones previously identified using sera from immunized animals. Two of the epitopic regions (including the C-terminal domain) showed increased reactivity with antibodies present in sera from patients with candidiasis as compared to control individuals. Patients who survived the infection di…

medicine.drug_classEnzyme-Linked Immunosorbent AssayMonoclonal antibodyMicrobiologyEpitopeImmunoglobulin GFungal ProteinsEpitopesMiceCandida albicansGeneticsmedicineAnimalsAmino Acid SequenceCandida albicansMolecular BiologyMice Inbred BALB CMembrane GlycoproteinsbiologyCandidiasisAntibodies Monoclonalbiology.organism_classificationDisseminated CandidiasisVirologyCorpus albicansProtein Structure TertiaryEpitope mappingbiology.proteinFemaleAntibodyEpitope MappingFEMS Microbiology Letters
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The estrogen receptor α:insulin receptor substrate 1 complex in breast cancer: structure–function relationships

2007

Background: Insulin receptor substrate 1 (IRS-1) is a signaling molecule that exerts a key role in mediating cross talk between estrogen receptor a (ERa) and insulin-like growth factor 1 (IGF-1) in breast cancer cells. Previously, we demonstrated that a fraction of IRS-1 binds ERa, translocates to the nucleus, and modulates ERa-dependent transcription at estrogen response elements (ERE). Here, we studied structure-function relationships of the ER-a:IRS-1 complex under IGF-1 and/or estradiol (E 2 ) stimulation. Materials and methods: ERa and IRS-1 deletion mutants were used to analyze structural and functional ERα/IRS-1 interactions. IRS-1 binding to ERE and IRS-1 role in ERa-dependent ERE t…

medicine.medical_specialtyInsulin Receptor Substrate ProteinsActive Transport Cell NucleusEstrogen receptorRepressorBreast NeoplasmsBiologyStructure-Activity Relationshipestrogen receptor alpha (ERa) Insulin receptor substrate 1 (IRS-1) breast cancerCell Line TumorInternal medicineCoactivatormedicineHumansInsulin-Like Growth Factor IReceptors InterferonEstradiolEstrogen Receptor alphaHematologyDNA-binding domainPhosphoproteinsPeptide FragmentsReceptor InsulinProtein Structure TertiaryCell biologyIRS1Repressor ProteinsPleckstrin homology domainEndocrinologyOncologyInsulin Receptor Substrate ProteinsFemaleChromatin immunoprecipitationProtein BindingAnnals of Oncology
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Pharmacological Characterization of Loss of Function Mutations of the Human Melanocortin 1 Receptor That Are Associated with Red Hair

2004

Variation in skin color is the major host risk factor for melanoma and other forms of skin cancer. Individuals with red hair show an increased ratio of phaeomelanin to eumelanin in both hair and skin. This ratio is regulated by the melanocortin (MC) 1 receptor. There are several common point mutations in the human MC1 receptor that are overrepresented in North European red-heads, and in individuals with pale skin. In order to determine the functional significance of these mutations, we expressed the Asp84Glu, Val92Met, Arg163Gln, and Asp294His variants of the human MC1 receptors in eukaryotic cells and determined their ability to bind alpha-melanocyte stimulating hormone (MSH) peptides and …

medicine.medical_specialtyMelanocyte-stimulating hormoneMolecular Sequence DataDermatologyBiologyKidneymedicine.disease_causeBiochemistrypolymorphismStructure-Activity RelationshipGPCRInternal medicineCyclic AMPmedicineHumansPoint MutationpigmentationAmino Acid SequencemelanocortinHair ColorReceptorMSHMolecular BiologyCells CulturedG protein-coupled receptorMutationintegumentary systemMelanomaPoint mutationCell Biologymedicine.diseaseProtein Structure TertiaryEndocrinologyalpha-MSHMelanocortinReceptor Melanocortin Type 1Melanocortin 1 receptorJournal of Investigative Dermatology
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Current perspectives on parathyroid hormone (PTH) and PTH-related protein (PTHrP) as bone anabolic therapies.

2013

Osteoporosis is characterized by low bone mineral density and/or poor bone microarchitecture leading to an increased risk of fractures. The skeletal alterations in osteoporosis are a consequence of a relative deficit of bone formation compared to bone resorption. Osteoporosis therapies have mostly relied on antiresorptive drugs. An alternative therapeutic approach for osteoporosis is currently available, based on the intermittent administration of parathyroid hormone (PTH). Bone anabolism caused by PTH therapy is mainly accounted for by the ability of PTH to increase osteoblastogenesis and osteoblast survival. PTH and PTH-related protein (PTHrP)-an abundant local factor in bone- interact wi…

medicine.medical_specialtyOsteoporosisParathyroid hormoneBone healingBiochemistryBone resorptionBone remodelingOsteogenesisInternal medicinemedicineAnimalsHumansBone regenerationCell ProliferationReceptor Parathyroid Hormone Type 1PharmacologyBone mineralOsteoblastsBone Density Conservation Agentsbusiness.industryParathyroid Hormone-Related ProteinOsteoblastCell Differentiationmedicine.diseaseProtein Structure Tertiarymedicine.anatomical_structureEndocrinologyGene Expression RegulationParathyroid HormoneOsteoporosisFemalebusinesshormones hormone substitutes and hormone antagonistsSignal TransductionBiochemical pharmacology
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