Search results for "Protein sequencing"

showing 7 items of 17 documents

Extracting similar sub-graphs across PPI Networks

2009

Singling out conserved modules (corresponding to connected sub-graphs) throughout protein-protein interaction networks of different organisms is a main issue in bioinformatics because of its potential applications in biology. This paper presents a method to discover highly matching sub-graphs in such networks. Sub-graph extraction is carried out by taking into account, on the one side, both protein sequence and network structure similarities and, on the other side, both quantitative and reliability information possibly available about interactions. The method is conceived as a generalization of a known technique, able to discover functional orthologs in interaction networks. Some preliminar…

Protein structure databaseBioinformatics network analysisProtein sequencingMatching (graph theory)GeneralizationComputer scienceReliability (computer networking)Protein function predictionGraph theoryData miningcomputer.software_genrecomputerNetwork analysis
researchProduct

Toward completion of the Earth’s proteome: an update a decade later

2017

Protein databases are steadily growing driven by the spread of new more efficient sequencing techniques. This growth is dominated by an increase in redundancy (homologous proteins with various degrees of sequence similarity) and by the incapability to process and curate sequence entries as fast as they are created. To understand these trends and aid bioinformatic resources that might be compromised by the increasing size of the protein sequence databases, we have created a less-redundant protein data set. In parallel, we analyzed the evolution of protein sequence databases in terms of size and redundancy. While the SwissProt database has decelerated its growth mostly because of a focus on i…

ProteomeOperations researchKnowledge Bases0206 medical engineering02 engineering and technologyComputational biologyBiology03 medical and health sciencesAnnotationProtein sequencingSequence Analysis ProteinThree-domain systemRedundancy (engineering)AnimalsHumansDatabases ProteinMolecular Biology030304 developmental biologySequence (medicine)0303 health sciencesComputational BiologyProteinsProtein superfamilyProteomeUniProtSoftware020602 bioinformaticsInformation SystemsBriefings in Bioinformatics
researchProduct

Assessing the low complexity of protein sequences via the low complexity triangle.

2020

Background Proteins with low complexity regions (LCRs) have atypical sequence and structural features. Their amino acid composition varies from the expected, determined proteome-wise, and they do not follow the rules of structural folding that prevail in globular regions. One way to characterize these regions is by assessing the repeatability of a sequence, that is, calculating the local propensity of a region to be part of a repeat. Results We combine two local measures of low complexity, repeatability (using the RES algorithm) and fraction of the most frequent amino acid, to evaluate different proteomes, datasets of protein regions with specific features, and individual cases of proteins…

ProteomeProteomesComputer scienceProtein SequencingBiochemistryDatabase and Informatics MethodsSequence Analysis ProteinProtein methodsPeptide sequencechemistry.chemical_classification0303 health sciencesSequenceMultidisciplinary030302 biochemistry & molecular biologyQRGenomicsAmino acidTandem RepeatsProteomeAmino Acid AnalysisMedicineSequence AnalysisResearch ArticleRepetitive Sequences Amino AcidBioinformaticsSequence analysisScienceResearch and Analysis MethodsGenome Complexity03 medical and health sciencesProtein DomainsAmino Acid Sequence AnalysisTandem repeatGeneticsHumansFraction (mathematics)Repeated SequencesAmino Acid SequenceMolecular Biology TechniquesSequencing TechniquesRepresentation (mathematics)Molecular Biology030304 developmental biologyMolecular Biology Assays and Analysis Techniquesbusiness.industryBiology and Life SciencesProteinsComputational BiologyPattern recognitionchemistryGlobular ProteinsArtificial intelligencebusinessPLoS ONE
researchProduct

Functional roles of the membrane-associated AAV protein MAAP

2021

AbstractWith a limited coding capacity of 4.7 kb, adeno-associated virus (AAV) genome has evolved over-lapping genes to maximise the usage of its genome. An example is the recently found ORF in the cap gene, encoding membrane-associated accessory protein (MAAP), located in the same genomic region as the VP1/2 unique domain, but in a different reading frame. This 13 KDa protein, unique to the dependovirus genus, is not homologous to any known protein. Our studies confirm that MAAP translation initiates from the first CTG codon found in the VP1 ORF2. We have further observed MAAP localised in the plasma membrane, in the membranous structures in close proximity to the nucleus and to the nuclea…

SciencevirusesGenetic VectorsBiologyVirus ReplicationGenomeinfektiotArticleVirusViral Proteins03 medical and health scienceschemistry.chemical_compoundCapsidGene therapyPlasmidProtein sequencingHumansGeneparvovirukset030304 developmental biology0303 health sciencesMultidisciplinaryMolecular engineeringVirus Assembly030302 biochemistry & molecular biologyQVirionRMembrane ProteinsTranslation (biology)DependovirusCell biologyCapsidchemistryMedicineCapsid ProteinsproteiinitDNAPlasmidskapsidi
researchProduct

Polynucleotide differentiation using hybrid solid-state nanopore functionalizing with α-hemolysin

2019

We report results from full atomistic molecular dynamics simulations on the properties of biomimetic nanopores. This latter result was obtained through the direct insertion of an α-hemolysin protein inside a hydrophobic solid-state nanopore. Upon translocation of different DNA strands, we demonstrate here that the theoretical system presents the same discrimination properties as the experimental one obtained previously. This opens an interesting way to promote the stability of a specific protein inside a solid nanopore to develop further biomimetic applications for DNA or protein sequencing.

Specific proteinPolynucleotidesSolid-state02 engineering and technologyMolecular Dynamics Simulation010402 general chemistry01 natural sciencesHemolysin ProteinsNanoporesMolecular dynamicschemistry.chemical_compoundProtein sequencingBiomimeticsAmino Acid SequenceChemistryHemolysinDNAGeneral Chemistry021001 nanoscience & nanotechnologyCondensed Matter Physics0104 chemical sciencesNanoporePolynucleotideBiophysics0210 nano-technologyHydrophobic and Hydrophilic InteractionsDNASoft Matter
researchProduct

Characterization of heat-labile toxin-subunit B from Escherichia coli by liquid chromatography-electrospray ionization-mass spectrometry and matrix-a…

2012

The possibilities of characterizing the heat-labile enterotoxin (LT) of enterotoxigenic Escherichia coli (ETEC) by liquid chromatography electrospray mass spectrometry (LC/ESI-MS) and matrix-assisted laser desorption with time-of-flight mass spectrometry (MALDI-TOF-MS) were investigated. The B subunit from recombinant E. coli (expression in Pichia pastoris) can be detected by LC/ESI-MS expressed in P. pastoris and the charge envelope signals can be observed; LC/ESI-MS and MALDI-TOF-MS analysis allowed the acquisition of labile toxin subunit B (LTB) molecular weight and preliminary structural characterization of LTB toxin. MALDI-TOF analysis after reduction and alkylation of the protein evid…

Spectrometry Mass Electrospray IonizationElectrospray ionizationProtein subunitBacterial ToxinsMolecular Sequence DataToxicologyMass spectrometrymedicine.disease_causespettroemtria di massaPichiaPichia pastorisEnterotoxinsProtein sequencingEnterotoxigenic Escherichia colimedicineTrypsinAmino Acid SequenceDisulfidesPhosphorylationEscherichia colitossinaChromatographyMolecular massbiologyChemistryEscherichia coli ProteinsE. coliGeneral Medicinebiology.organism_classificationRecombinant ProteinsMolecular WeightProtein SubunitsSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationFood ScienceChromatography LiquidFood and chemical toxicology : an international journal published for the British Industrial Biological Research Association
researchProduct

Polypeptide sequence of the chlorophyll a/b/c-binding protein of the prasinophycean alga Mantoniella squamata.

1994

The primary structure of the Chla/b/c-binding protein from Mantoniella squamata is determined. This is the first report that protein sequencing reveals one modified amino acid resulting in a LHCP-specific TFA-cleavage site. The comparison of the sequence of Mantoniella with other Chla/b-and Chla/c-binding proteins shows that the modified amino acid is located in a region which is highly conserved in all these proteins. The alignment also reveals that the LHCP of Mantoniella is related to the Chla/b-binding proteins. Finally, possible Chl-binding regions are discussed.

chemistry.chemical_classificationChlorophyll abiologyBinding proteinProtein primary structureCell BiologyPlant ScienceGeneral Medicinebiology.organism_classificationBiochemistryMolecular biologyAmino acidLight-harvesting complexchemistry.chemical_compoundProtein sequencingBiochemistrychemistryMantoniellaPeptide sequencePhotosynthesis research
researchProduct