Search results for "Molecular sequence"

showing 10 items of 1972 documents

Chloroplastic glutamine synthetase from Brassica napus.

1993

chemistry.chemical_classificationChloroplastsDatabases FactualPhysiologyMolecular Sequence DataNucleic acid sequenceBrassicaPlant ScienceBrassicaBiologyGenetic codebiology.organism_classificationGenes PlantChloroplastOpen Reading FramesEnzymechemistryBiochemistryGlutamate-Ammonia LigaseComplementary DNAGlutamine synthetaseGeneticsAmino Acid SequenceCarbon-Nitrogen LigasesResearch Article
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Retention behaviour of paracelsin peptides on reversed-phase silicas with varying n-alkyl chain length and ligand density.

1989

As part of further investigations on the characterization of the ligand-induced conformational stabilization of peptides, two series of n-alkyldimethylsilyl bonded silicas have been prepared. In series A the n-alkyl chain length, n, of the bonded phase was varied between 1 and 20 carbon atoms at a constant ligand density. In series B the ligand density, alpha exp, was gradually changed from 0 to 4.1 mumol/m2 on a C1, C4, C6, C8 and C18 bonded phase. The retention behaviour of four peptides of the paracelsin family were examined under isocratic conditions, using a ternary mobile phase of water-methanol-acetonitrile (22:39:39, v/v/v). Plots of k' versus n showed pronounced maxima between n = …

chemistry.chemical_classificationChromatographyLigandChemistryOrganic ChemistryMolecular Sequence DataTemperaturePeptideGeneral MedicineLigandsBiochemistryAnalytical ChemistryHydrophobic effectPartition coefficientPhase (matter)Spectrophotometry UltravioletAmino Acid SequenceTernary operationSelectivityPeptidesAlkylChromatography High Pressure LiquidAntimicrobial Cationic PeptidesJournal of chromatography
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Glutamine synthetase from roots of Brassica napus. Nucleotide sequence of a cytosolic isoform.

1994

chemistry.chemical_classificationGene isoformDNA ComplementarybiologyBase SequencePhysiologyMolecular Sequence DataBrassicaNucleic acid sequencePlant ScienceBrassicabiology.organism_classificationGenes PlantIsoenzymesCytosolEnzymeCytosolchemistryBiochemistryGlutamate-Ammonia LigaseComplementary DNAGlutamine synthetaseGeneticsCarbon-Nitrogen LigasesResearch ArticlePlant physiology
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Detection of RNA modifications

2010

RNA nucleotide modifications are typically of low abundance and frequently go unnoticed by standard detection methods of molecular biology and cell biology. With a burst of knowledge intruding from such diverse areas as genomics, structural biology, regulation of gene expression and immunology, it becomes increasingly clear that many exciting functions of nucleotide modifications remain to be explored. It follows in turn that the biology of nucleotide modification and editing is a field poised to rapidly gain importance in a variety of fields. The detection and analysis of nucleotide modifications present a clear limitation in this respect. Here, various methods for detection of nucleotide …

chemistry.chemical_classificationGeneticsBase SequenceNucleotidesMolecular Sequence DataRNACell BiologyComputational biologyBiologyEnzymeschemistryAbundance (ecology)RNANucleotideRNA Processing Post-TranscriptionalMolecular BiologyRNA Biology
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Sequence of a new tRNALeu(U∗AA) from brewer's yeast

1991

The nucleotide sequence of a new tRNA(Leu)(anticodon U*AA) from Saccharomyces cerevisiae which could recognize exclusively the UUA codon has been determined. Its primary structure is: pGGAGGGUUGm2GCac4CGAGDGmGDCDAAGGCm2(2)GGCAGACmUU*AAm1GA++ + psi CUGUUGGACGGUUGUCCGm5CGCGAGT psi CGm1A(orA)ACCUCGCAUCCUUCACCA. This tRNA has a large extraloop and contains 15 modified nucleotides. So far it is the third isoacceptor tRNA for leucine in yeast. It has 61% homology with tRNA(Leu)(anticodon m5CAA) and 63% homology with tRNA(Leu)(anticodon UAG), the two other known yeast tRNAs(Leu).

chemistry.chemical_classificationGeneticsRNA Transfer LeuBase SequencebiologyMolecular Sequence DataSaccharomyces cerevisiaeNucleic acid sequenceProtein primary structureSaccharomyces cerevisiaeGeneral Medicinebiology.organism_classificationBiochemistryYeastHomology (biology)BiochemistrychemistryTransfer RNANucleic Acid ConformationElectrophoresis Gel Two-DimensionalNucleotideLeucineCodonBiochimie
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Structure of a polysaccharide from the lipopolysaccharide of Vibrio vulnificus clinical isolate YJ016 containing 2-acetimidoylamino-2-deoxy-L-galactu…

2009

Abstract A polysaccharide isolated after mild acid degradation of the lipopolysaccharide of Vibrio vulnificus clinical isolate YJ016 was found to contain l -Fuc, d -GlcpNAc, 2,4-diacetamido-2,4,6-trideoxy- d -glucose (di-N-acetylbacillosamine, d -QuiNAc4NAc), and 2-acetimidoylamino-2-deoxy- l -galacturonic acid ( l -GalNAmA). The last sugar derivative was confirmed by correlations for nitrogen-linked protons in 2D TOCSY and ROESY spectra measured in a H2O–D2O mixture. The following structure of the polysaccharide was established by 1H and 13C NMR spectroscopy, including 2D ROESY and 1H,13C HMBC experiments: Download : Download full-size image where the degree of 6-O-acetylation of the later…

chemistry.chemical_classificationLipopolysaccharidesMagnetic Resonance SpectroscopybiologyLipopolysaccharideChemistryStereochemistryOrganic ChemistryMolecular Sequence DataPolysaccharides BacterialGeneral MedicineVibrio vulnificusbiology.organism_classificationPolysaccharideBiochemistryAnalytical ChemistrySugar derivativesResidue (chemistry)chemistry.chemical_compound13c nmr spectroscopyBiochemistryCarbohydrate SequenceGalacturonic acidVibrio vulnificusCarbohydrate research
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Conformational studies of hexapeptides containing two dehydroamino acid residues in positions 2 and 5 in peptide chain

2008

Conformational preferences of a group of hexapeptides containing two dehydroamino acid residues in Positions 2 and 5 in peptide chain were investigated by means of spectroscopic methods (NMR and CD) and theoretical calculations. In the case of dimethylsulfoxide (DMSO) solution, only peptide with free N-termini adopted rigid 310-helical conformation, for the rest of examined peptides extended and “zig-zag” conformers were predominant. CD measurements showed that only in chloroform solution the conformational freedom of investigated peptides was restricted. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 691–699, 2008. This article was originally published online as an accepted preprint. The “…

chemistry.chemical_classificationMagnetic Resonance SpectroscopyProtein ConformationStereochemistryCircular DichroismMolecular Sequence DataOrganic ChemistryTemperatureBiophysicsPeptideGeneral MedicineAmidesBiochemistryProtein Structure SecondaryBiomaterialschemistry.chemical_compoundChain (algebraic topology)chemistryDehydroalanineAmino Acid SequenceAmino AcidsProtonsPeptidesConformational isomerismBiopolymers
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Synthesis of β-d-mannosides from β-d-glucosides via an intramolecular Sn2 reaction at C-2

1992

Abstract The selective synthesis of β- d -mannosides was achieved by first synthesizing β- d -glucosides that carry a N -phenylcarbamoyl protecting group at O-3. These derivatives were transformed into the corresponding β- d -mannosides by intramolecular nucleophilic substitution with inversion of configuration at C-2, the O -triflyl group being the leaving group. Subsequent intramolecular attack of the neighboring carbamoyl group resulted in the formation of the 2,3-carbonate of the desired β d -mannoside.

chemistry.chemical_classificationMannosidesIntramolecular reactionStereochemistryMolecular Sequence DataOrganic ChemistryLeaving groupGeneral MedicineBiochemistryAnalytical ChemistryCarbohydrate SequenceGlucosidesIsomerismAldosechemistryMannosidesIntramolecular forceNucleophilic substitutionSN2 reactionProtecting groupGlycoproteinsCarbohydrate Research
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Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation.

1996

The Bowman-Birk inhibitor from soybean is a small protein that contains a binary arrangement of trypsin-reactive and chymotrypsin-reactive subdomains. In this report, the crystal structure of this anticarcinogenic protein has been determined to 0.28-nm resolution by molecular replacement from crystals grown at neutral pH. The crystal structure differs from a previously determined NMR structure [Werner, M. H. & Wemmer, D. E. (1992) Biochemistry 31, 999-1010] in the relative orientation of the two enzyme-insertion loops, in some details of the main chain trace, in the presence of favourable contacts in the trypsin-insertion loop, and in the orientation of several amino acid side chains. The p…

chemistry.chemical_classificationModels MolecularMagnetic Resonance SpectroscopyStereochemistryProtein ConformationMolecular Sequence DataWaterCrystal structureCrystallography X-RayBiochemistryProtein tertiary structureProtein Structure SecondaryAmino acidCrystallographychemistry.chemical_compoundKineticsProtein structurechemistrySide chainChymotrypsinProtein foldingMolecular replacementAmino Acid SequenceBifunctionalTrypsin Inhibitor Bowman-Birk SoybeanEuropean journal of biochemistry
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Amino acid sequence and homology modeling of obtustatin, a novel non-RGD-containing short disintegrin isolated from the venom of Vipera lebetina obtu…

2003

Disintegrins represent a group of cysteine-rich peptides occurring in Crotalidae and Viperidae snake venoms, and are potent antagonists of several integrin receptors. A novel disintegrin, obtustatin, was isolated from the venom of the Vipera lebetina obtusa viper, and represents the first potent and selective inhibitor of the binding of integrin alpha(1)beta(1) to collagen IV. The primary structure of obtustatin contains 41 amino acids and is the shortest disintegrin described to date. Obtustatin shares the pattern of cysteines of other short disintegrins. However, in contrast to known short disintegrins, the integrin-binding loop of obtustatin is two residues shorter and does not express t…

chemistry.chemical_classificationModels MolecularbiologyDisintegrinsMolecular Sequence DataProtein primary structureVenomViper VenomsViper VenomsBiochemistryAmino acidBiochemistrychemistryViperidaebiology.animalFor the RecordDisintegrinbiology.proteinViperidaeAnimalsHomology modelingAmino Acid SequenceMolecular BiologyPeptide sequenceOligopeptides
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