Search results for "Native state"

showing 10 items of 12 documents

Leading role of the sea urchin Arbacia lixula in maintaining the barren state in southwestern Mediterranean

2011

Sympatric sea urchin species are usually considered to belong to the same grazer guild. Nevertheless, their role in community dynamics may vary due to species-specific morphological traits, feeding preferences and foraging behavior. In the Mediterranean Sea, the two species Paracentrotus lividus and Arbacia lixula co-occur in barren areas. Whereas P. lividus is usually considered responsible for creating a barren ground, the roles of the two sea urchin species in its maintenance are currently unclear. The relative and combined effects of P. lividus and A. lixula on maintaining the benthic community in the barren state were tested experimentally, using orthogonal exclusion of the two species…

0106 biological sciencesSea urchinEcologybiologyEcologyalteranative states010604 marine biology & hydrobiologyForagingMedierranean SeaAquatic Sciencebiology.organism_classification010603 evolutionary biology01 natural sciencesParacentrotus lividusMediterranean seaBenthic zoneSympatric speciationbiology.animalGuild14. Life underwaterSea urchinArbacia lixulaEcology Evolution Behavior and SystematicsMarine Biology
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The Boson Peak of Amyloid Fibrils: Probing the Softness of Protein Aggregates by Inelastic Neutron Scattering

2014

Proteins and polypeptides are characterized by low-frequency vibrations in the terahertz regime responsible for the so-called "boson peak". The shape and position of this peak are related to the mechanical properties of peptide chains. Amyloid fibrils are ordered macromolecular assemblies, spontaneously formed in nature, characterized by unique biological and nanomechanical properties. In this work, we investigate the effects of the amyloid state and its polymorphism on the boson peak. We used inelastic neutron scattering to probe low-frequency vibrations of the glucagon polypeptide in the native state and in two different amyloid morphologies in both dry and hydrated sample states. The dat…

AmyloidPhysics::Biological PhysicsQuantitative Biology::BiomoleculesChemistryProtein dynamicsNeutron diffractionNeutron scatteringProtein aggregationFibrilVibrationAmyloid Protein dynamics collective motions boson peakInelastic neutron scatteringSurfaces Coatings and FilmsNeutron DiffractionMicroscopy Electron TransmissionChemical physicsMolecular vibrationSpectroscopy Fourier Transform InfraredMaterials ChemistryNative statePhysical and Theoretical ChemistryAtomic physics
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Trehalose effects on α-crystallin aggregates

2007

alpha-Crystallin in its native state is a large, heterogeneous, low-molecular weight (LMW) aggregate that under certain conditions may progressively became part of insoluble high-molecular weight (HMW) systems. These systems are supposed to play a relevant role in eye lens opacification and vision impairment. In this paper, we report the effects of trehalose on alpha-crystallin aggregates. The role of trehalose in alpha-crystallin stress tolerance, chaperone activity and thermal stability is studied. The results show that trehalose stabilizes the alpha-crystallin native structure, inhibits alpha-crystallin aggregation, and disaggregates preformed LMW systems not affecting its chaperone acti…

BiophysicsMicroscopy Atomic ForceBiochemistrythermal stabilitychemistry.chemical_compoundCrystallinNative stateThermal stabilityBenzothiazolesalpha-Crystallinsalpha-crystallinChaperone activityProtein Structure QuaternaryEye lensMolecular BiologyNative structureCircular DichroismTrehalosefood and beveragesCell BiologyTrehaloseeye diseaseschaperone activityThiazolesSpectrometry FluorescencechemistryBiochemistryaggregatesα-Crystallin Trehalose Aggregates Chaperone activity Thermal stabilitysense organsBiochemical and Biophysical Research Communications
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Probing DNA conductivity with photoinduced electron transfer and scanning tunneling microscopy.

2012

Abstract The possibility that the stacked DNA bases can mediate vectorial electron transfer has been examined using two different approaches. Experiments on photoinduced electron transfer with intercalated donors and acceptors (either randomly bound or linked dyads of ruthenium complex and viologen) indicate that while DNA may be a better medium than acetonitrile for electron transfer over short distances (2-3-base pair, equivalent to 10-14Å centre-to-centre separation), it is a poor medium for transport over larger separations. Attempts to measure conductivity of individual DNA molecules using scanning tunneling microscopy to image mixed monolayers of mercaptohexanol (MCH) and 30-mer or 10…

ChemistryViologenElectronsGeneral MedicineDNAPhotochemistryElectron transport chainPhotoinduced electron transferIntercalating Agentslaw.inventionElectron TransportElectron transferStructural BiologylawMicroscopy Scanning TunnelingMonolayerMicroscopymedicineNative stateScanning tunneling microscopeMolecular BiologyOxidation-Reductionmedicine.drugJournal of biomolecular structuredynamics
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Isolation and characterization of haemoporin, an abundant haemolymph protein from Aplysia californica.

2003

In the present study, we show the isolation and characterization of the protein haemoporin, which constitutes the second most abundant protein fraction in the haemolymph of the marine gastropod Aplysia californica. Although Aplysia is commonly used to investigate the molecular basis of learning, not much is known about the proteins in its haemolymph, which is in contact with the neurons owing to the open circulatory system of molluscs. In the native state, haemoporin is a macromolecular complex forming a cylinder with a central solvent-filled pore. The native complex most probably is a homopentamer made up from 70 kDa subunits with a molecular mass of 360 kDa and a sedimentation coefficient…

Circular dichroismanimal structuresMolecular Sequence DataMegathura crenulataBiochemistrySequence Analysis ProteinHemolymphHemolymphAplysiaNative stateAnimalsAmino Acid SequenceMolecular BiologyProtein secondary structurebiologyMolecular massCircular DichroismCell BiologyAnatomyBlood Proteinsbiology.organism_classificationMolecular WeightMicroscopy ElectronSpectrometry FluorescenceBiochemistryAplysiaProtein quaternary structureElectrophoresis Polyacrylamide GelUltracentrifugationResearch ArticleThe Biochemical journal
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Native-state pea albumin and globulin behavior upon transglutaminase treatment

2015

International audience; The behavior of pea albumin (Alb) and globulin (Glob) in their native state upon microbial transglutaminase (MTGase) treatment was studied. Only Glob was able to form a gel, at up to a 10% (w/w) concentration, with a minimum gelling concentration of 6% (w/w), and with a cross-linking degree of 25%. The most affected Glob subunits were convicilin (71 kDa), vicilins (55, 50, and 35 kDa), and legumin acidic subunit (40 kDa). In contrast, the legumin basic subunit (20 kDa) and vicilins of molecular weight less than 20 kDa remained mostly intact in all studied conditions. The cross-linking degree of Alb was 12%, which was not sufficient to form MTGase-induced gel. Major a…

GlobulinTissue transglutaminaseProtein subunitBioengineering01 natural sciencesApplied Microbiology and BiotechnologyBiochemistry0404 agricultural biotechnologyNative stateLeguminPea albuminsDenaturation (biochemistry)[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCross-linking degreebiologyChemistry010401 analytical chemistryAlbuminglob (programming)04 agricultural and veterinary sciences040401 food scienceOptimum parameters0104 chemical sciencesBiochemistryPea globulinsbiology.proteinMicrobial transglutaminase properties
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Local dynamic properties of the heme pocket in native and solvent-induced molten-globule-like states of cytochrome c

2002

We report the Soret absorption band, down to cryogenic temperature, of native and molten-globule-like state of horse heart cytochrome c. The band profile is analyzed in terms of vibronic coupling of the heme normal modes to the electronic transition in the framework of the Franck-Condon approximation. From the temperature dependence of the Gaussian broadening and of the peak position, we obtain information on the 'bath' of low frequency harmonic motions of the heme group within the heme pocket. The reported data indicate that, compared to the native state, the less rigid tertiary structure of the molten globule is reflected in a higher flexibility of the heme pocket and in greater conformat…

GlycerolProtein FoldingHot TemperatureCytochromeProtein ConformationBiophysicsCytochrome c GroupHemeProtein dynamicsBiochemistrychemistry.chemical_compoundMolten-globule proteinsNative stateSettore BIO/10HemeBinding SitesbiologySpectrum AnalysisProtein dynamicsOrganic ChemistryMolten globuleOptical absorption spectroscopyCrystallographyVibronic couplingchemistryAbsorption bandbiology.proteinMolten-globule proteins; Optical absorption spectroscopy; Protein dynamicsProtein foldingMathematics
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Response of the oxygen sensor NreB to air in vivo: Fe-S-containing NreB and apo-NreB in aerobically and anaerobically growing Staphylococcus carnosus.

2009

ABSTRACT The sensor kinase NreB from Staphylococcus carnosus contains an O 2 -sensitive [4Fe-4S] 2+ cluster which is converted by O 2 to a [2Fe-2S] 2+ cluster, followed by complete degradation and formation of Fe-S-less apo-NreB. NreB·[2Fe-2S] 2+ and apoNreB are devoid of kinase activity. NreB contains four Cys residues which ligate the Fe-S clusters. The accessibility of the Cys residues to alkylating agents was tested and used to differentiate Fe-S-containing and Fe-S-less NreB. In a two-step labeling procedure, accessible Cys residues in the native protein were first labeled by iodoacetate. In the second step, Cys residues not labeled in the first step were alkylated with the fluorescent…

Iron-Sulfur ProteinsbiologyAerobic bacteriaStaphylococcusGene Expression Regulation BacterialAlkylationbiology.organism_classificationMicrobiologyModels BiologicalAerobiosisOxygenBiochemistryBacterial ProteinsSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationNative stateImmunoprecipitationAnaerobic bacteriaAnaerobiosisCysteineKinase activityMolecular BiologyBacteriaCysteineStaphylococcus carnosusSignal TransductionJournal of bacteriology
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Time-dependent monomerization of bacteriorhodopsin in triton X-100 solutions analyzed by high-performance liquid chromatography

1984

Abstract Bacteriorhodopsin from Halobacterium halobium was monomerized in Triton X-100 solutions. The process of delipidation was monitored by size-exclusion high-performance liquid chromatography under conditions that preserved the native conformation of the protein. The effects on the process of monomerization of the concentration and pH of the Triton X-100 solutions were investigated. The monomeric bacteriorhodopsin separated was active in light-dependent proton translocation when incorporated into soy bean lecithin liposomes.

Liposomefood.ingredientChromatographybiologyOrganic ChemistryPhotoproteinBacteriorhodopsinGeneral Medicinebiology.organism_classificationBiochemistryHigh-performance liquid chromatographyLecithinAnalytical Chemistrychemistry.chemical_compoundfoodchemistrybiological sciencesTriton X-100biology.proteinNative stateHalobacteriaceaeJournal of Chromatography A
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Decoding the Folding of Burkholderia glumae Lipase: Folding Intermediates En Route to Kinetic Stability

2012

The lipase produced by Burkholderia glumae folds spontaneously into an inactive near-native state and requires a periplasmic chaperone to reach its final active and secretion-competent fold. The B. glumae lipase-specific foldase (Lif) is classified as a member of the steric-chaperone family of which the propeptides of alpha-lytic protease and subtilisin are the best known representatives. Steric chaperones play a key role in conferring kinetic stability to proteins. However, until present there was no solid experimental evidence that Lif-dependent lipases are kinetically trapped enzymes. By combining thermal denaturation studies with proteolytic resistance experiments and the description of…

Macromolecular AssembliesProtein StructureProtein FoldingBurkholderiaProtein ConformationStereochemistryBiophysicslcsh:MedicineBiochemistryProtein Chemistrybacterial lipasemolten globuleBacterial ProteinsNative stateBurkholderia glumaeLipaseProtein Interactionslcsh:ScienceBiologyMultidisciplinarybiologylipase-specific foldasePhysicslcsh:RSubtilisinProteinsLipasebiology.organism_classificationMolten globuleEnzymesChaperone ProteinsKineticsBiochemistryChaperone (protein)Enzyme StructureProteolysisFoldasebiology.proteinlcsh:Qsteric chaperoneProtein foldingnear-native folding intermediateResearch ArticleMolecular Chaperones
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