Search results for "Structural Biology."

showing 10 items of 822 documents

REP2: A Web Server to Detect Common Tandem Repeats in Protein Sequences

2020

Ensembles of tandem repeats (TRs) in protein sequences expand rapidly to form domains well suited for interactions with proteins. For this reason, they are relatively frequent. Some TRs have known structures and therefore it is advantageous to predict their presence in a protein sequence. However, since most TRs diverge quickly, their detection by classical sequence comparison algorithms is not very accurate. Previously, we developed a method and a web server that used curated profiles and thresholds for the detection of 11 common TRs. Here we present a new web server (REP2) that allows the analysis of TRs in both individual and aligned sequences. We provide currently precomputed analyses f…

Repetitive Sequences Amino AcidWeb serverProteomeComputer scienceComputational biologycomputer.software_genreEvolution Molecular03 medical and health sciences0302 clinical medicineTandem repeatStructural BiologySequence comparisonHumansAmino Acid SequenceMolecular BiologyConserved Sequence030304 developmental biologySequence (medicine)Comparative genomicsInternet0303 health sciencesMultiple sequence alignmentBacteriaProteinsTandem Repeat SequencesProteomeUniProtSequence Alignmentcomputer030217 neurology & neurosurgeryJournal of Molecular Biology
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Cloning of a novel putative G-protein-coupled receptor (NLR) which is expressed in neuronal and lymphatic tissue.

1993

AbstractA novel G-protein-coupled receptor was isolated from mouse and rat neuronal and lymphatic tissues. The amino acid sequence of the rat receptor (rNLR) shows an overall homology of 80% to a recently cloned receptor from Burkitt's lymphoma cells (BLR1) which is exclusively expressed in lymphatic tissues [(1992) Eur. J. Immunol. 22, 2795]. Much less homology between rNLR and BLR1 was observed at the N-terminus (about 40%), whereas rNLR and the mouse homologue mNLR show 92% amino acid identity. Northern blot analysis of NLR revealed a predominant 5.5 kb mRNA species in various brain regions and neuronal cell lines, whereas in the spleen a 3 kb transcript is predominant. This distribution…

Restriction MappingInterleukin 8BiochemistryReceptors G-Protein-CoupledMiceStructural BiologyTumor Cells CulturedLymphocytesCloning MolecularReceptorPeptide sequencechemistry.chemical_classificationNeuronsGenomic LibraryBurkitt's lymphomaBrainBurkitt LymphomaPolymerase chain reactionAmino acidOligodeoxyribonucleotidesOrgan SpecificityG-protein-coupled receptorBLR1Molecular Sequence DataBiophysicsReceptors Cell SurfaceBiologyNLRGTP-Binding ProteinsComplementary DNAGeneticsmedicineAnimalsHumansNorthern blotAmino Acid SequenceRNA MessengerMolecular BiologyG protein-coupled receptorMessenger RNABase SequenceSequence Homology Amino AcidCell Biologymedicine.diseaseMolecular biologyIntronsRatsNG108-15 cellchemistryBurkitt's lymphomaFEBS letters
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Toward oxygen binding curves of single respiratory proteins

2004

Oxygen binding curves of single molecules promise to discriminate between different models describing cooperativity because load distributions are accessible. Individual tarantula hemocyanins could be detected by fluorescence correlation spectroscopy using intrinsic tryptophan fluorescence as sensor of bound oxygen. However, imaging of immobilized proteins was not possible due to fast photo-bleaching. It is shown that tetra-methyl-carboxy-rhodamine (TAMRA), commonly used as a fluorescence label in single-molecule spectroscopy, can also be applied to monitor bound oxygen. The dye's fluorescence is quenched due to Förster energy transfer to the oxygenated active sites of hemocyanin.

Rhodaminesmedicine.medical_treatmentAnalytical chemistryGeneral Physics and Astronomychemistry.chemical_elementSpidersHemocyaninFluorescence correlation spectroscopyCooperativityCell BiologyFluorescenceOxygenOxygenchemistryStructural BiologyHemocyaninsmedicineBiophysicsAnimalsMoleculeGeneral Materials ScienceSpectroscopyOxygen bindingFluorescent DyesMicron
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Rhodopsin transport in the membrane of the connecting cilium of mammalian photoreceptor cells

2000

The transport of the photopigment rhodopsin from the inner segment to the photosensitive outer segment of vertebrate photoreceptor cells has been one of the main remaining mysteries in photoreceptor cell biology. Because of the lack of any direct evidence for the pathway through the photoreceptor cilium, alternative extracellular pathways have been proposed. Our primary aim in the present study was to resolve rhodopsin trafficking from the inner to the outer segment. We demonstrate, predominantly by high-sensitive immunoelectron microscopy, that rhodopsin is also densely packed in the membrane of the photoreceptor connecting cilium. Present prominent labeling of rhodopsin in the ciliary mem…

RhodopsinOpsingenetic structuresPhotoreceptor Connecting CiliumImmunoblottingMolecular Sequence Datamacromolecular substancesMyosinsBiologyPhotoreceptor cellRats Sprague-DawleyMiceRetinal Rod Photoreceptor CellsStructural BiologymedicineAnimalsHumansPhotopigmentAmino Acid SequenceCiliaMicroscopy ImmunoelectronCiliary membraneCiliumRod OpsinsAntibodies MonoclonalDyneinsBiological TransportCell BiologyMiddle AgedRod Cell Outer SegmentActin cytoskeletonImmunohistochemistryActinseye diseasesRatsCell biologyMice Inbred C57BLmedicine.anatomical_structureRhodopsinMyosin VIIabiology.proteinCattleFemalesense organsRetinitis PigmentosaCell Motility and the Cytoskeleton
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A general strategy to determine the congruence between a hierarchical and a non-hierarchical classification

2007

This article is available from: http://www.biomedcentral.com/1471-2105/8/442

Saccharomyces cerevisiae ProteinsComputer scienceDecision treecomputer.software_genrelcsh:Computer applications to medicine. Medical informaticsInteractomeBiochemistryPattern Recognition AutomatedMitochondrial ProteinsUser-Computer InterfaceSimilarity (network science)Structural BiologyArtificial IntelligenceSequence Analysis ProteinProtein Interaction MappingCluster AnalysisDatabases Proteinlcsh:QH301-705.5Molecular BiologyOligonucleotide Array Sequence AnalysisApplied MathematicsMethodology ArticleDendrogramDecision TreesReproducibility of ResultsClassificationPartition (database)Computer Science ApplicationsTree (data structure)Rankinglcsh:Biology (General)Pattern recognition (psychology)lcsh:R858-859.7Data miningcomputerBiological networkBMC Bioinformatics
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Role of glycine-82 as a pivot point during the transition from the inactive to the active form of the yeast Ras2 protein

1991

AbstractRas proteins bind either GDP or GTP with high affinity. However, only the GTP-bound form of the yeast Ras2 protein is able to stimulate adenylyl cyclase. To identify amino acid residues that play a role in the conversion from the GDP-bound to the GTP-bound state of Ras proteins, we have searched for single amino acid substitutions that selectively affected the binding of one of the two nucleotides. We have found that the replacement of glycine-82 of the Ras2 protein by serine resulted in an increased rate of dissociation of Gpp(NH)p, a nonhydrolysable analog of GTP, while the GDP dissociation rate was not significantly modified. Glycine-82 resides in a region that is highly conserve…

Saccharomyces cerevisiae ProteinsGTP'Guanosine diphosphateProtein ConformationRestriction MappingGlycineBiophysicsSaccharomyces cerevisiaeBiochemistryFungal ProteinsGTP-binding protein regulatorsProtein structureGTP-Binding ProteinsStructural BiologyEscherichia coliGeneticsRHO protein GDP dissociation inhibitorAmino Acid SequenceRas2Binding siteMolecular BiologyPeptide sequencechemistry.chemical_classificationGuanylyl ImidodiphosphateBinding SitesPoint mutationChemistryCell BiologyGuanosine triphosphateRecombinant ProteinsAmino acidModels StructuralBiochemistryMutagenesis Site-Directedras ProteinsS. cerevisaePlasmidsRasFEBS Letters
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Bromodomain factor 1 (Bdf1) protein interacts with histones

2001

AbstractUsing a yeast two-hybrid assay we detected an interaction between the N-terminal region of histone H4 (amino acids 1–59) and a fragment of the bromodomain factor 1 protein (Bdf1p) (amino acids 304–571) that includes one of the two bromodomains of this protein. No interaction was observed using fragments of histone H4 sequence smaller than the first 59 amino acids. Recombinant Bdf1p (rBdf1p) demonstrates binding affinity for histones H4 and H3 but not H2A and H2B in vitro. Moreover, rBdf1p is able to bind histones H3 and H4 having different degrees of acetylation. Finally, we have not detected histone acetyltransferase activity associated with Bdf1p.

Saccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsBiophysicsBromodomainTwo-hybridBiochemistryFungal ProteinsHistonesHistone H4SaccharomycesAcetyltransferasesGenes ReporterStructural BiologyTwo-Hybrid System TechniquesHistone methylationHistone H2AGeneticsHistone acetyltransferase activityHistone octamerMolecular BiologyHistone AcetyltransferasesBromodomain factor 1 proteinbiologyChemistryCell BiologyHistone acetyltransferasePeptide FragmentsChromatinBromodomainHistoneBiochemistryPCAFbiology.proteinHistone acetyltransferaseProtein BindingTranscription FactorsFEBS Letters
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The C-terminal region of the Hot1 transcription factor binds GGGACAAA-related sequences in the promoter of its target genes

2015

Response to hyperosmotic stress in the yeast Saccharomyces cerevisiae involves the participation of the general stress response mediated by Msn2/4 transcription factors and the HOG pathway. One of the transcription factors activated through this pathway is Hot1, which contributes to the control of the expression of several genes involved in glycerol synthesis and flux, or in other functions related to adaptation to adverse conditions. This work provides new data about the interaction mechanism of this transcription factor with DNA. By means of one-hybrid and electrophoretic mobility assays, we demonstrate that the C-terminal region, which corresponds to amino acids 610-719, is the DNA-bindi…

Saccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsGenes FungalMolecular Sequence DataResponse elementBiophysicsE-boxSequence alignmentSaccharomyces cerevisiaeBiologyBiochemistryConserved sequenceOsmoregulationStructural BiologyGene Expression Regulation FungalGeneticsComputer SimulationAmino Acid SequenceDNA FungalPromoter Regions GeneticMolecular BiologyTranscription factorConserved SequenceSequence DeletionCis-regulatory moduleGeneticsBinding SitesBase SequenceSequence Homology Amino AcidMembrane Transport ProteinsPromoterDNA-binding domainProtein Structure TertiaryMutationSequence AlignmentProtein BindingTranscription FactorsBiochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms
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Energetic aspects of intramolecular coupling between the nucleotide binding site and the distal switch II region of the yeast RAS2 protein

1994

AbstractWe have studied the interaction of the yeast RAS2 protein with guanine nucleotides using energetic parameters for the dissociation of RAS·nucleotide complexes. The results indicated that a Gly → Ser substitution at position 82 led to an altered interaction with GppNHp and, to a lesser extent, also with GDP. It was also possible to conclude that structural perturbation of Gly82 can stimulate nucleotide release by decreasing the energetic barrier for nucleotide dissociation. This, together with the observation that residues 80 and 81 are involved in the response of RAS to nucleotide exchange factors without affecting GDP binding per se, suggests a potential mechanism for exchange fact…

Saccharomyces cerevisiae ProteinsStereochemistryCdc25GuanineSaccharomyces cerevisiaeGlycineBiophysicsSaccharomyces cerevisiaeGuanosine DiphosphateBiochemistryFungal ProteinsStructure-Activity RelationshipSCD25chemistry.chemical_compoundGTP-Binding ProteinsStructural BiologyEscherichia coliSerineGeneticsNucleotideBinding siteRas2Molecular Biologychemistry.chemical_classificationGuanylyl ImidodiphosphateBinding SitesCDC25biologyGDP bindingTemperatureCell Biologybiology.organism_classificationGuanine NucleotidesRecombinant ProteinsYeastchemistryras ProteinsGDP exchange factorbiology.proteinThermodynamicsRASFEBS Letters
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Yeast HAT1 and HAT2 deletions have different life-span and transcriptome phenotypes

2005

AbstractHAT-B is a yeast histone acetyltransferase composed of Hat1, Hat2 and Hif1 proteins. We demonstrate that a hat2 mutant or a hat1hat2 double mutant, but not a hat1 mutant, have an extended life-span. Transcriptome analysis shows that the single hat mutants are not very different from wild type. However, the comparison of the hat1 and hat2 transcriptomes shows that they are different. The hat1hat2 double mutant shows a transcriptional phenotype similar to that of the hat1 mutant but strongly enhanced. These results indicate that Hat2p could have additional functions in the cell to those of Hat1p.

Saccharomyces cerevisiae ProteinsTranscription GeneticHAT-BMutantBiophysicsSaccharomyces cerevisiaeBiochemistryTranscriptomeDNA-chipAcetyltransferasesStructural BiologyHat2Life-spanGeneticsImmunoprecipitationSirtuinsMolecular BiologyHistone AcetyltransferasesGeneticsbiologyWild typeCell BiologyHistone acetyltransferaseTelomereHat1PhenotypeYeastPhenotypebiology.proteinHistone deacetylaseHAT1Gene DeletionFEBS Letters
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