Search results for "genetics [Transcriptome]"

showing 10 items of 3033 documents

Novel 3D bio-macromolecular bilinear descriptors for protein science: Predicting protein structural classes

2015

In the present study, we introduce novel 3D protein descriptors based on the bilinear algebraic form in the ℝn space on the coulombic matrix. For the calculation of these descriptors, macromolecular vectors belonging to ℝn space, whose components represent certain amino acid side-chain properties, were used as weighting schemes. Generalization approaches for the calculation of inter-amino acidic residue spatial distances based on Minkowski metrics are proposed. The simple- and double-stochastic schemes were defined as approaches to normalize the coulombic matrix. The local-fragment indices for both amino acid-types and amino acid-groups are presented in order to permit characterizing fragme…

Models MolecularProtein structural classesMathematical parametersProtein functionQuantitative Structure-Activity RelationshipBilinear interpolationQuantitative structure activity relation3D protein descriptorBilinear formProceduresChemical structureStatistical parametersMinkowski spaceProtein analysisAmino AcidsPriority journalMathematicsInterpretabilityQuantitative Biology::BiomoleculesApplied MathematicsStatistical parameterValidation studyGeneral MedicineComputer simulationDiscriminant analysisReproducibilityAmino acidAlgorithmChemistryProtein conformationModeling and SimulationStatistical modelGeneral Agricultural and Biological SciencesBiological systemAmino acid analysisAlgorithmsNonbiological modelStatistics and ProbabilityCorrelation coefficientLDAMacromolecular SubstancesMarkov chainMacromoleculeStructure analysisModels BiologicalArticleGeneral Biochemistry Genetics and Molecular BiologyCombinatoricsStochastic processesBilinear formBiologyMatrixGeneral Immunology and MicrobiologyProteinCoulombic matrixComputational BiologyProteinsReproducibility of ResultsLinear discriminant analysisWeightingCorrelation coefficientProtein structureBiological modelLinear ModelsThree-dimensional modelingJournal of Theoretical Biology
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Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion

2001

The structural protein VP6 of rotavirus, an important pathogen responsible for severe gastroenteritis in children, forms the middle layer in the triple-layered viral capsid. Here we present the crystal structure of VP6 determined to 2 A resolution and describe its interactions with other capsid proteins by fitting the atomic model into electron cryomicroscopic reconstructions of viral particles. VP6, which forms a tight trimer, has two distinct domains: a distal beta-barrel domain and a proximal alpha-helical domain, which interact with the outer and inner layer of the virion, respectively. The overall fold is similar to that of protein VP7 from bluetongue virus, with the subunits wrapping …

Models MolecularRotavirusCations DivalentViral proteinvirusesMolecular Sequence DataHemagglutinins ViralTrimerCrystal structureBiologyCrystallography X-Raymedicine.disease_causeProtein Structure SecondaryArticleGeneral Biochemistry Genetics and Molecular BiologyVirus03 medical and health sciencesCapsidRotavirusAtomic modelmedicineAnimalsAmino Acid SequenceAntigens ViralMolecular BiologyPeptide sequence030304 developmental biology0303 health sciencesSequence Homology Amino AcidGeneral Immunology and Microbiology030306 microbiologyViral Core ProteinsGeneral NeuroscienceVirionvirus diseasesMolecular biologyZincCapsidSolventsBiophysicsCapsid ProteinsCattleThe EMBO Journal
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Molecular modelling study of the role of cholesterol in the stimulation of the oxytocin receptor.

2001

Cholesterol, an integral component of membranes in Eucaryota, is a modifier of membrane properties. In vivo studies have demonstrated that cholesterol can also modulate activities of some G protein-coupled receptors (GPCRs), which are integral membrane proteins. This can result either from an effect of cholesterol on the membrane fluidity or from specific interactions of the membrane cholesterol with the receptor, as recently demonstrated for the cholecystokinin type beta (CCKRbeta) or the oxytocin receptor (OTR). Using molecular modelling, we studied conformational preferences of cholesterol and several of its analogues. Subsequently, we simulated the distributions of their preferred confo…

Models MolecularSequence Homology Amino AcidProtein ConformationMolecular Sequence DataBiologyCholecystokinin receptorOxytocin receptorGeneral Biochemistry Genetics and Molecular BiologySterolSterolsCholesterolBiochemistryReceptors OxytocinMutationBiophysicsMembrane fluidityHumansAmino Acid SequenceReceptorCholecystokininIntegral membrane proteinhormones hormone substitutes and hormone antagonistsCholecystokininG protein-coupled receptorProtein BindingActa biochimica Polonica
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Nucleotide's bilinear indices: Novel bio-macromolecular descriptors for bioinformatics studies of nucleic acids. I. Prediction of paromomycin's affin…

2009

A new set of nucleotide-based bio-macromolecular descriptors are presented. This novel approach to bio-macromolecular design from a linear algebra point of view is relevant to nucleic acids quantitative structure-activity relationship (QSAR) studies. These bio-macromolecular indices are based on the calculus of bilinear maps on Re(n)[b(mk)(x (m),y (m)):Re(n) x Re(n)--Re] in canonical basis. Nucleic acid's bilinear indices are calculated from kth power of non-stochastic and stochastic nucleotide's graph-theoretic electronic-contact matrices, M(m)(k) and (s)M(m)(k), respectively. That is to say, the kth non-stochastic and stochastic nucleic acid's bilinear indices are calculated using M(m)(k)…

Models MolecularStatistics and ProbabilityPure mathematicsQuantitative structure–activity relationshipParomomycinMolecular Sequence DataDNA FootprintingQuantitative Structure-Activity RelationshipBilinear interpolationGeneral Biochemistry Genetics and Molecular BiologyInterpretation (model theory)DNA PackagingLinear regressionOrder (group theory)MathematicsStochastic ProcessesBase SequenceGeneral Immunology and MicrobiologyApplied MathematicsComputational BiologyGeneral MedicineModeling and SimulationDNA ViralLinear algebraStandard basisHIV-1Nucleic acidRNA ViralGeneral Agricultural and Biological SciencesAlgorithmJournal of Theoretical Biology
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5-(3,4-Dimethoxybenzyl)-7-isopropyl-1,3,5-triazepane-2,6-dione acetonitrile solvate refined using a multipolar atom model

2010

International audience; The crystal structure of the title compound, C16H23N3O4·CH3CN, was refined using a multipolar atom model transferred from an experimental electron-density database. The refinement showed some improvement in crystallographic statistical indices compared with the independent atom model. The triazepane ring adopts a twist-boat conformation. In the crystal structure, the mol­ecule forms inter­molecular contacts with 14 different neighbours. There are two N-H...O and one C-H...O inter­molecular hydrogen bond.

Models MolecularStereochemistryMolecular ConformationCrystal structure010402 general chemistryRing (chemistry)Crystallography X-Ray01 natural sciencesGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundBenzyl Compounds[CHIM.CRIS]Chemical Sciences/CristallographyMoleculeAcetonitrileQuantitative Biology::Biomolecules010405 organic chemistryChemistryHydrogen bondIntermolecular forceGeneral MedicineAzepines0104 chemical sciencesCrystallographySolubilityDimerizationIsopropylAtom model
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Comprehensive analysis of a Vibrio parahaemolyticus strain extracellular serine protease VpSP37

2015

Proteases play an important role in the field of tissue dissociation combined with regenerative medicine. During the years new sources of proteolytic enzymes have been studied including proteases from different marine organisms both eukaryotic and prokaryotic. Herein we have purified a secreted component of an isolate of Vibrio parahaemolyticus, with electrophoretic mobilities corresponding to 36 kDa, belonging to the serine proteases family. Sequencing of the N-terminus enabled the in silico identification of the whole primary structure consisting of 345 amino acid residues with a calculated molecular mass of 37.4 KDa. The purified enzyme, named VpSP37, contains a Serine protease domain be…

Models MolecularTMPRSS6Proteasesmedicine.medical_treatmentMolecular Sequence Datalcsh:MedicineBiologySettore BIO/19 - Microbiologia GeneraleSubstrate SpecificitySerine03 medical and health sciencesSettore BIO/10 - BiochimicamedicineAnimalsAmino Acid Sequencelcsh:Science030304 developmental biologySerine protease0303 health sciencesMultidisciplinaryProteaseEelsVibrio parahaemolyticuBiochemistry Genetics and Molecular Biology (all)030306 microbiologyAnimalMedicine (all)lcsh:RProteolytic enzymesEelVibrio InfectionTrypsinMolecular biology3. Good healthBiochemistryAgricultural and Biological Sciences (all)Vibrio InfectionsAmino Acid Sequence; Animals; Eels; Models Molecular; Molecular Sequence Data; Sequence Alignment; Serine Proteases; Substrate Specificity; Vibrio Infections; Vibrio parahaemolyticus; Agricultural and Biological Sciences (all); Biochemistry Genetics and Molecular Biology (all); Medicine (all)biology.proteinlcsh:QVibrio parahaemolyticusSerine ProteaseSerine ProteasesSequence AlignmentMASP1medicine.drugResearch Article
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N-[tert-Butoxycarbonylglycyl-(Z)-α,β-dehydrophenylalanylglycyl-(E)-α,β-dehydrophenylalanylphenylalanyl]-4-nitroaniline ethanol solvate

2005

The alpha,beta-dehydrophenylalanine residues influence the conformation of the title pentapeptide Boc0-Gly1-Delta(Z)Phe2-Gly3-Delta(E)Phe4-L-Phe5-p-NA ethanol solvate, C42H43N7O9.C2H5OH. The first unsaturated phenylalanyl (Delta(Z)Phe2) and the third glycyl (Gly3) residues form a type I beta turn, while the second unsaturated phenylalanyl (Delta(E)Phe4) and the last phenylalanyl (L-Phe5) residues are part of a type II beta turn. All the amino acids in the peptide are linked trans to one another. The crystal structure is stabilized by intra- and intermolecular hydrogen bonds.

Models Molecularchemistry.chemical_classificationOligopeptideAniline CompoundsEthanolMolecular StructureHydrogen bondStereochemistryPeptideGeneral MedicineCrystal structureCrystallography X-RayPentapeptide repeatGeneral Biochemistry Genetics and Molecular BiologyAmino acidchemistry.chemical_compoundchemistryMoleculeOligopeptidesActa Crystallographica Section C Crystal Structure Communications
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Bis(diethylenetriamine-κ3N)nickel(II) 5-amino-1,3,4-thiadiazole-2-sulfonamidate chloride monohydrate

2000

In the X-ray crystal structure of the title complex, [Ni(C(4)H(13)N(3))(2)](C(2)H(3)N(4)O(2)S(2))Cl.H(2)O, the coordination polyhedron is composed of non-centrosymmetric [Ni(diethylenetriamine)(2)](2+) cations in which the triamine ligands coordinate to the metal centre as tridentate ligands in a facial position. The Ni(II) ions are linked to six N atoms in an octahedral arrangement, slightly compressed in one extreme. The sulfonamide behaves as a counter-ion instead of as a ligand. Important information about the deprotonated sulfonamide group conformation has been obtained.

Models Molecularchemistry.chemical_classificationSulfonamidesStereochemistryLigandchemistry.chemical_elementHydrogen BondingGeneral MedicineCrystal structureCrystallography X-RayMedicinal chemistryGeneral Biochemistry Genetics and Molecular BiologySulfonamidechemistry.chemical_compoundNickelchemistryOctahedronDiethylenetriamineOrganometallic CompoundsAmine gas treatingDiazoCarbonic Anhydrase InhibitorsActa Crystallographica Section C Crystal Structure Communications
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A supramolecular system that strictly follows the binding mechanism of conformational selection

2020

Induced fit and conformational selection are two dominant binding mechanisms in biology. Although induced fit has been widely accepted by supramolecular chemists, conformational selection is rarely studied with synthetic systems. In the present research, we report a macrocyclic host whose binding mechanism is unambiguously assigned to conformational selection. The kinetic and thermodynamic aspects of this system are studied in great detail. It reveals that the kinetic equation commonly used for conformational selection is strictly followed here. In addition, two mathematical models are developed to determine the association constants of the same guest to the two host conformations. A “confo…

Models Molecularconformational selectionProtein ConformationScienceSupramolecular chemistrybiological systemsGeneral Physics and Astronomy010402 general chemistryLigands01 natural sciencesGeneral Biochemistry Genetics and Molecular BiologyBiophysical PhenomenaArticlesupramolecular chemistryMolecular recognitionProtein structureProtein DomainsComputational chemistryHeterocyclic Compoundsmechanisms in biologysupramolekulaarinen kemialcsh:ScienceSelection (genetic algorithm)Multidisciplinary010405 organic chemistryMechanism (biology)QProteinsGeneral ChemistryModels Theoretical0104 chemical sciencesKineticsPhysical chemistryKinetic equationsProteins metabolismsynthetic systemsThermodynamicslcsh:Qmolecular recognitionSupramolecular chemistryProtein Binding
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Interaction of Circadian Clock Proteins CRY1 and PER2 Is Modulated by Zinc Binding and Disulfide Bond Formation

2014

SummaryPeriod (PER) proteins are essential components of the mammalian circadian clock. They form complexes with cryptochromes (CRY), which negatively regulate CLOCK/BMAL1-dependent transactivation of clock and clock-controlled genes. To define the roles of mammalian CRY/PER complexes in the circadian clock, we have determined the crystal structure of a complex comprising the photolyase homology region of mouse CRY1 (mCRY1) and a C-terminal mouse PER2 (mPER2) fragment. mPER2 winds around the helical mCRY1 domain covering the binding sites of FBXL3 and CLOCK/BMAL1, but not the FAD binding pocket. Our structure revealed an unexpected zinc ion in one interface, which stabilizes mCRY1-mPER2 int…

Models Molecularendocrine systemanimal structuresPeriod (gene)Molecular Sequence DataCircadian clockBiologyCrystallography X-RayGeneral Biochemistry Genetics and Molecular BiologyMiceCryptochromeAnimalsProtein Interaction Domains and MotifsAmino Acid SequenceCircadian rhythmBinding siteBiochemistry Genetics and Molecular Biology(all)F-Box ProteinsPeriod Circadian ProteinsRecombinant ProteinsCryptochromesPER2ZincBiochemistryFAD bindingBiophysicsPeriod Circadian ProteinsSequence AlignmentCell
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