Search results for " Quaternary"

showing 10 items of 148 documents

Quaternary structure and molecular model of a 4x6mer arthropod hemocyanin in oxygenated and deoxygenated states by 3D cryo-electron microscopy

2007

Extended abstract of a paper presented at MC 2007, 33rd DGE Conference in Saarbrücken, Germany, September 2 – September 7, 2007

CrystallographyMolecular modelbiologyChemistryCryo-electron microscopymedicine.medical_treatmentBiophysicsmedicineProtein quaternary structureHemocyaninArthropodbiology.organism_classificationInstrumentationMicroscopy and Microanalysis
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Quaternary transition pathway in sol–gel encapsulated haemoglobin tracked by NIR and UV spectral relaxations

2008

→T structural transition of haemoglobin (hb), the protein responsible for oxygen (o) transport in the red blood cells of vertebrates, is the hall mark example. This transition, which regu lates o2 uptake in the lungs and o2 release in the tissues, is a switch in the quaternary structure of the protein from a low-affinity state (T) to a high-affinity state (R), two well-characterised structures. The struc tural pathway connecting the end states of this transition remains unclear, however, although recently several experimental 1 or

CrystallographyTransition (genetics)quaternary relaxationChemistryStereochemistryprotein dynamicchemistry.chemical_elementProtein quaternary structureStructural transitionQuaternaryOxygensol-gel encapsulationSol-gel
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Pulsed EPR determination of water accessibility to spin-labeled amino acid residues in LHCIIb.

2009

Membrane proteins reside in a structured environment in which some of their residues are accessible to water, some are in contact with alkyl chains of lipid molecules, and some are buried in the protein. Water accessibility of residues may change during folding or function-related structural dynamics. Several techniques based on the combination of pulsed electron paramagnetic resonance (EPR) with site-directed spin labeling can be used to quantify such water accessibility. Accessibility parameters for different residues in major plant light-harvesting complex IIb are determined by electron spin echo envelope modulation spectroscopy in the presence of deuterated water, deuterium contrast in …

DetergentsBiophysicsLight-Harvesting Protein ComplexesSpectroscopy Imaging and Other TechniquesBuffersCrystallography X-RaySpectral linelaw.inventionlawMoleculeHumansAmino AcidsElectron paramagnetic resonanceProtein Structure QuaternaryHyperfine structureAlkylPlant Proteinschemistry.chemical_classificationPulsed EPRChemistryElectron Spin Resonance SpectroscopyPeasTemperatureWaterSite-directed spin labelingCrystallographyDeuteriumSolubilityMutationSolventsSpin LabelsProtein MultimerizationBiophysical journal
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Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein pore.

2006

High susceptibility of rabbit erythrocytes toward the pore-forming action of staphylococcal alpha-toxin correlates with the presence of saturable, high affinity binding sites. All efforts to identify a protein or glycolipid receptor have failed, and the fact that liposomes composed solely of phosphatidylcholine are efficiently permeabilized adds to the enigma. A novel concept is advanced here to explain the puzzle. We propose that low affinity binding moieties can assume the role of high affinity binding sites due to their spatial arrangement in the membrane. Evidence is presented that phosphocholine head groups of sphingomyelin, clustered in sphingomyelin-cholesterol microdomains, serve th…

ErythrocytesPhosphorylcholineBacterial ToxinsBiologyBiochemistryCell Linechemistry.chemical_compoundHemolysin ProteinsGlycolipidMembrane MicrodomainsPhosphatidylcholineAnimalsHumansReceptorProtein Structure QuaternaryMolecular BiologyPhosphocholineLiposomeBinding SitesCell BiologySphingomyelinsMembraneCholesterolSphingomyelin PhosphodiesteraseBiochemistrychemistryLiposomesRabbitsSphingomyelinFunction (biology)Protein BindingThe Journal of biological chemistry
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The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness.

2021

- Single-spanning SARS-CoV-2 envelope (E) protein topology is a major determinant of protein quaternary structure and function. - Charged residues distribution in E protein sequences from highly pathogenic human coronaviruses (i.e., SARS-CoV, MERS-CoV and SARS-CoV-2) stabilize Ntout-Ctin membrane topology. - E protein sequence could have evolved to ensure a more robust membrane topology from MERS-CoV to SARS-CoV and SARS-CoV-2.

EvolutionvirusesBiophysicsBBA Research Lettermedicine.disease_causeBiochemistryEnvelope proteinCell membraneEvolution Molecular03 medical and health sciencesCoronavirus Envelope ProteinsProtein sequencingmedicineHumansskin and connective tissue diseasesProtein Structure Quaternary030304 developmental biologyCoronavirus0303 health sciencesChemistrySARS-CoV-2030302 biochemistry & molecular biologyfungiCell MembraneRobustness (evolution)virus diseasesCell Biologyrespiratory tract diseasesCoronavirusmedicine.anatomical_structureMembrane topologyMembrane topologyBiophysicsProtein quaternary structureProtein topologyFunction (biology)Biochimica et biophysica acta. Biomembranes
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Structural and functional diversity of the lectin repertoire in teleost fish: Relevance to innate and adaptive immunity

2011

Protein–carbohydrate interactions mediated by lectins have been recognized as key components of innate immunity in vertebrates and invertebrates, not only for recognition of potential pathogens, but also for participating in downstream effector functions, such as their agglutination, immobilization, and complement-mediated opsonization and killing. More recently, lectins have been identified as critical regulators of mammalian adaptive immune responses. Fish are endowed with virtually all components of the mammalian adaptive immunity, and are equipped with a complex lectin repertoire. In this review, we discuss evidence suggesting that: (a) lectin repertoires in teleost fish are highly dive…

Fish ProteinsModels MolecularImmunologySettore BIO/05 - ZoologiaBiologyAdaptive ImmunityArticleImmune systemPhagocytosisC-type lectinAntifreeze ProteinsLectinsAnimalsLectins Innate immunity Fish Self/non-self recognition Effector Regulatory functions Complement activationProtein Structure QuaternaryAntigens ViralComplement ActivationMannan-binding lectinAntigens BacterialInnate immune systemBacteriaEffectorFishesLectinComplement System ProteinsOpsonin ProteinsAcquired immune systemInvertebratesImmunity InnateComplement systemCell biologyProtein Structure TertiaryGene Expression RegulationOrgan SpecificityVertebratesVirusesbiology.proteinDevelopmental Biology
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Ten Years of Paleoceanographic Studies at ODP Site 963 (Central Mediterranean Sea)

2014

The geographical location, the shape and the circulation pattern makes the Mediterranean Sea an ideal laboratory to study the interplay between different climatic systems, abrupt climate changes and the response of marine ecosystems. The Ocean Drilling Program Site 963 was drilled in the Northwestern part of the Sicily Channel, the sill that divides the western from the eastern Mediterranean Sea. Numerous papers have been published on Site 963 sediments in the last decade, investigating Mediterranean paleoceanographic themes. Here we offer a synthetic framework of these investigations carried out by sub-centennial resolution. We present the whole sequence of suborbital climatic oscillations…

ForaminiferaDeep chlorophyll maximumCoccolithophores late quaternary mediterranean sea planktonic foraminifera.OceanographyMediterranean seabiologyInterglacialDeglaciationMarine ecosystemStadialbiology.organism_classificationGeologyTeleconnection
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Structural stability and properties of three isoforms of the major light-harvesting chlorophyll a/b complexes of photosystem II.

2008

AbstractThree isoforms of the major light-harvesting chlorophyll (Chl) a/b complexs of photosystem II (LHCIIb) in the pea, namely, Lhcb1, Lhcb2, and Lhcb3, were obtained by overexpression of apoprotein in Escherichia coli and by successfully refolding these isoforms with thylakoid pigments in vitro. The sequences of the protein, pigment stoichiometries, spectroscopic characteristics, thermo- and photostabilities of different isoforms were analysed. Comparison of their spectroscopic properties and structural stabilities revealed that Lhcb3 differed strongly from Lhcb1 and Lhcb2 in both respects. It showed the lowest Qy transition energy, with its reddest absorption about 2 nm red-shifted, an…

Gene isoformChlorophyllChlorophyll aProtein FoldingPhotosystem IIBiophysicsLight-Harvesting Protein ComplexesPhotochemistryBiochemistryThylakoidsReconstitutionchemistry.chemical_compoundPigmentPigment stoichiometryEscherichia coliThermal stabilityMajor light-harvesting chlorophyll a/b complex of photosystem IIProtein Structure QuaternaryThermostabilityPlant ProteinsChlorophyll APeasPhotosystem II Protein ComplexCell BiologyRecombinant ProteinsIsoenzymeschemistryPhotostabilityChlorophyllThylakoidvisual_artBiophysicsvisual_art.visual_art_mediumThermostabilityBiochimica et biophysica acta
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Hemocyanin subunit organization of the gastropod Rapana thomasiana

1999

Abstract RtH1 and RtH2, the two hemocyanin isoforms of the prosobranch gastropod Rapana thomasiana, have been purified by anion-exchange chromatography and studied by SDS–PAGE and immunoelectrophoresis. Both subunit types are built up of eight functional units (FUs). Under reducing conditions subunit RtH2 splits into two fragments, RtH2- a – f and RtH2- gh, suggesting the presence of a disulfide bridge between FU2- f and FU2- g. By proteolytic cleavage of the subunits into three-, two-, and single-FU fragments, purification of fragments by HPLC, N-terminal sequencing of the peptides, and crossed-line immunoelectrophoresis, FUs- a – h of RtH2 and FU- a, FU- d, FU- e, and FU- f of RtH1 were i…

Gene isoformSubunitProtein subunitmedicine.medical_treatmentMolecular Sequence DataBiophysicsImmunoelectrophoresisBiologyMegathura crenulataCleavage (embryo)BiochemistryHigh-performance liquid chromatographyHemocyaninRapana thomasianamedicineAnimalsProtein IsoformsAmino Acid SequenceProtein Structure QuaternaryMolecular BiologyGasteropodsmedicine.diagnostic_testPancreatic ElastaseImmunochemistryStructureHemocyaninbiology.organism_classificationMolecular biologyPeptide FragmentsMolluscaHemocyanin; Gasteropods; Structure; SubunitHemocyaninsImmunoelectrophoresis Two-Dimensional
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The European Pine Marten Martes martes (Linnaeus, 1758) Is Autochthonous in Sicily and Constitutes a Well-Characterised Major Phylogroup within the S…

2022

No molecular data are currently available for the Sicilian populations of the European pine marten Martes martes, thus preventing any sound inference about its native or non-native status on the island, as well as the local phylogeography of the species. In order to investigate these issues, we sequenced two mtDNA markers in road-killed specimens collected in Sicily. Both markers consistently demonstrated the existence of a well-characterised Sicilian clade of the species, which is endemic to the island and constitutes the sister group of a clade including the Mediterranean and Central–North European major phylogroups of the European pine marten. Such evidence supports the autochthony of Ma…

General Veterinarybiodiversity on islandsSettore BIO/05 - ZoologiaAnimal Science and Zoologymitochondrial DNAPleistocene refugiaQuaternary glaciationsPleistocene refugia; biodiversity on islands; mitochondrial DNA; Quaternary glaciationsAnimals; Volume 12; Issue 19; Pages: 2546
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