Search results for "Structural Biology."

showing 10 items of 822 documents

Corrigendum to: α-Conotoxins EpI and AuIB switch subtype selectivity and activity in native versus recombinant nicotinic acetylcholine receptors (FEB…

2003

Corrigendum to: K-Conotoxins EpI and AuIB switch subtype selectivity and activity in native versus recombinant nicotinic acetylcholine receptors (FEBS 27779) [FEBS Letters 554 (2003) 219^223]C Annette Nickea;1, Marek Samochockib, Marion L. Loughnana, Paramjit S. Bansala, Alfred Maelickeb, Richard J. Lewisa; aInstitute for Molecular Bioscience, University of Queensland, Brisbane, Qld. 4072, Australia bInstitute for Physiological Chemistry and Pathobiochemistry, University of Mainz, D-55099 Mainz, Germany First published online 24 December 2003

ChemistryBiophysicsSubtype selectivityCell BiologyPharmacologyBiochemistrylaw.inventionNicotinic agonistGanglion type nicotinic receptorStructural BiologylawPhysiological chemistryGeneticsRecombinant DNAAlpha-4 beta-2 nicotinic receptorMolecular BiologyAcetylcholine receptorα conotoxinFEBS Letters
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Excitation modes for fourier transform-ion cyclotron resonance mass spectrometry.

1992

AbstractVarious geometric configurations for the excitation of coherent ion motion in Fourier transform-ion cyclotron resonance mass spectrometry (FT-ICR/MS) are analyzed (in some cases for the first time) with unified notation. The instantaneous power absorption, F·v, in which v is ion velocity and F the force produced by the applied excitation electric field (harmonic, single frequency, on-resonance, in-phase), is time averaged and then set equal to the time rate of change of ion total (cyclotron + magnetron + trapping) energy, to yield a differential equation that is readily solved for the (time-dependent) amplitude of each of the various ion motions. The standard FT-ICR excitation (name…

ChemistryCyclotronAnalytical chemistryCyclotron resonanceMass spectrometryFourier transform ion cyclotron resonanceIonlaw.inventionAmplitudeStructural BiologylawPhysics::Plasma PhysicsAtomic physicsSpectroscopyIon cyclotron resonanceExcitationJournal of the American Society for Mass Spectrometry
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The Root effect—a physiological perspective

2004

ChemistryPerspective (graphical)FishesRoot effectGeneral Physics and AstronomyCell BiologyHydrogen-Ion ConcentrationPseudobranchOxygenFisheryHemoglobinsStructural BiologyAnimalsFish <Actinopterygii>General Materials ScienceMicron
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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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Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein 1 1Edited by A. R. Fersht

1999

Negative factor (Nef) is a regulatory myristoylated protein of human immunodeficiency virus (HIV) that has a two-domain structure consisting of an anchor domain and a core domain separated by a specific cleavage site of the HIV proteases. For structural analysis, the HIV-1 Nef anchor domain (residues 2-57) was synthesized with a myristoylated and non-myristoylated N terminus. The structures of the two peptides were studied by1H NMR spectroscopy and a structural model was obtained by restrained molecular dynamic simulations. The non-myristoylated peptide does not have a unique, compactly folded structure but occurs in a relatively extended conformation. The only rather well-defined canonical…

ChemistryViral proteinStereochemistrySequence alignmentmedicine.disease_causeSerineCrystallographyProtein structureStructural BiologyHelixmedicinelipids (amino acids peptides and proteins)Molecular BiologyProtein secondary structurePeptide sequenceMyristoylationJournal of Molecular Biology
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Down-regulation of early sea urchin histone H2A gene relies on cis regulative sequences located in the 5' and 3' regions and including the enhancer b…

2004

The tandem repeated sea urchin alpha-histone genes are developmentally regulated by gene-specific promoter elements. Coordinate transcription of the five genes begins after meiotic maturation of the oocyte, continues through cleavage, and reaches its maximum at morula stage, after which these genes are shut off and maintained in a silenced state for the life cycle of the animal. Although cis regulative sequences affecting the timing and the level of expression of these genes have been characterized, much less is known about the mechanism of their repression. Here we report the results of a functional analysis that allowed the identification of the sequence elements needed for the silencing …

Chloramphenicol O-Acetyltransferaseanimal structuresEmbryo NonmammalianMicroinjectionsgenomic insulatorDown-RegulationSettore BIO/11 - Biologia MolecolareBiologyRegulatory Sequences Nucleic AcidDNA-binding proteinHistonesStructural BiologyTranscription (biology)Gene expressionHistone H2Atranscriptional repressionGene silencingAnimalsGene SilencingTransgenesEnhancerPromoter Regions GeneticMolecular BiologyGenePsychological repressionhistone geneRepetitive Sequences Nucleic AcidSequence DeletionGeneticsenhancer blockerGastrulaEnhancer Elements GeneticSea Urchinsembryonic structuresProtein BindingJournal of molecular biology
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Folding in vitro of light-harvesting chlorophyll a/b protein is coupled with pigment binding.

2002

The major light-harvesting chlorophyll a/b protein (LHCIIb) of the plant photosynthetic apparatus is able to self-organise in vitro. When the recombinant apoprotein, Lhcb1, is solubilised in the denaturing detergent sodium (or lithium) dodecylsulfate (SDS or LDS) and then mixed with chlorophylls and carotenoids under renaturing conditions, structurally authentic LHCIIb forms. Assembly of functional LHCIIb, as indicated by the establishment of energy transfer between complex-bound chlorophyll molecules, occurs in two apparent kinetic steps with time constants of 10 to 30 seconds and 50 to 300 seconds, depending on the reaction conditions. Here, we use circular dichroism (CD) in the far-UV ra…

Chlorophyll aCircular dichroismProtein FoldingCircular DichroismPigment bindingProtein domainPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesPhotochemistryPhotosynthesisProtein Structure SecondaryRecombinant Proteinschemistry.chemical_compoundPigmentchemistryStructural BiologyChlorophyllvisual_artvisual_art.visual_art_mediumMolecular BiologyProtein secondary structureMicellesSequence DeletionJournal of molecular biology
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Consecutive binding of chlorophylls a and b during the assembly in vitro of light-harvesting chlorophyll-a/b protein (LHCIIb).

2006

The apoprotein of the major light-harvesting chlorophyll a/b complex (LHCIIb) is post-translationally imported into the chloroplast, where membrane insertion, protein folding, and pigment binding take place. The sequence and molecular mechanism of the latter steps is largely unknown. The complex spontaneously self-organises in vitro to form structurally authentic LHCIIb upon reconstituting the unfolded recombinant protein with the pigments chlorophyll a, b, and carotenoids in detergent micelles. Former measurements of LHCIIb assembly had revealed two apparent kinetic phases, a faster one (tau1) in the range of 10 s to 1 min, and a slower one (tau2) in the range of several min. To unravel th…

Chlorophyll bChlorophyllChlorophyll aTime FactorsPigment bindingLight-Harvesting Protein ComplexesModels BiologicalFluorescencechemistry.chemical_compoundStructural BiologyChlorophyll bindingAnimalsProtein Structure QuaternaryMolecular BiologyChlorophyll ACircular DichroismLight-harvesting complexes of green plantsChloroplastB vitaminsKineticsBiochemistrychemistryEnergy TransferChlorophyllBiophysicsChlamydomonas reinhardtiiProtein BindingJournal of molecular biology
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Chlorophyll b is involved in long-wavelength spectral properties of light-harvesting complexes LHC I and LHC II.

2001

AbstractChlorophyll (Chl) molecules attached to plant light-harvesting complexes (LHC) differ in their spectral behavior. While most Chl a and Chl b molecules give rise to absorption bands between 645 nm and 670 nm, some special Chls absorb at wavelengths longer than 700 nm. Among the Chl a/b-antennae of higher plants these are found exclusively in LHC I. In order to assign this special spectral property to one chlorophyll species we reconstituted LHC of both photosystem I (Lhca4) and photosystem II (Lhcb1) with carotenoids and only Chl a or Chl b and analyzed the effect on pigment binding, absorption and fluorescence properties. In both LHCs the Chl-binding sites of the omitted Chl species…

Chlorophyll bChlorophyllPhotosystem IIPigment bindingPhotosynthetic Reaction Center Complex ProteinsBiophysicsLight-Harvesting Protein ComplexesPhotosystem IPhotochemistryBiochemistryAbsorptionLight-harvesting complexReconstitutionchemistry.chemical_compoundSolanum lycopersicumStructural BiologySpinacia oleraceaGeneticsChlorophyll bindingCentrifugation Density GradientMolecular BiologyChlorophyll fluorescenceLong-wavelength chlorophyllBinding SitesPhotosystem I Protein ComplexChemistryChlorophyll ATemperaturePhotosystem II Protein ComplexLight-harvesting complexes of green plantsCell BiologyPigments BiologicalPlant LeavesSpectrometry FluorescenceLight-harvesting complexChlorophyll fluorescenceChlorophyll bindingProtein BindingFEBS letters
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Effects of chlorophyll a, chlorophyll b, and xanthophylls on the in vitro assembly kinetics of the major light-harvesting chlorophyll a/b complex, LH…

2001

The major light-harvesting chlorophyll a/b complex (LHCIIb) of photosystem II in higher plants can be reconstituted with pigments in lipid-detergent micelles. The pigment-protein complexes formed are functional in that they perform efficient internal energy transfer from chlorophyll b to chlorophyll a. LHCIIb formation in vitro, can be monitored by the appearance of energy transfer from chlorophyll b to chlorophyll a in time-resolved fluorescence measurements. LHCIIb is found to form in two apparent kinetic steps with time constants of about 30 and 200 seconds. Here we report on the dependence of the LHCIIb formation kinetics on the composition of the pigment mixture used in the reconstitut…

Chlorophyll bchemistry.chemical_classificationChlorophyll afood and beveragesLight-harvesting complexes of green plantsPhotochemistrychemistry.chemical_compoundB vitaminschemistryNeoxanthinStructural BiologyChlorophyllXanthophyllChlorophyll bindingMolecular BiologyJournal of Molecular Biology
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