Search results for "Low complexity"

showing 10 items of 11 documents

Characterization of MRNP34, a novel methionine-rich nacre protein from the pearl oysters

2012

9 pages; International audience; Nacre of the Pinctada pearl oyster shells is composed of 98% CaCO(3) and 2% organic matrix. The relationship between the organic matrix and the mechanism of nacre formation currently constitutes the main focus regarding the biomineralization process. In this study, we isolated a new nacre matrix protein in P. margaritifera and P. maxima, we called Pmarg- and Pmax-MRNP34 (methionine-rich nacre protein). MRNP34 is a secreted hydrophobic protein, which is remarkably rich in methionine, and which is specifically localised in mineralizing the epithelium cells of the mantle and in the nacre matrix. The structure of this protein is drastically different from those …

0106 biological sciencesBiomineralizationCalcifying mantleMethionine-richMolecular Sequence DataClinical BiochemistryGene ExpressionBiologyMatrix (biology)engineering.materialProteomics010603 evolutionary biology01 natural sciencesBiochemistryLow complexity03 medical and health sciencesPaleontologychemistry.chemical_compoundCalcification PhysiologicMethionineAnimalsAmino Acid SequencePinctada[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsNacre030304 developmental biology0303 health sciencesMethionineViral matrix proteinOrganic ChemistryProteinsEpithelial Cells[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/Biomaterialsbiology.organism_classificationProtein Structure TertiarychemistryBiochemistryengineeringMolluscMatrix proteinPearlBiomineralizationPinctada
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Disentangling the complexity of low complexity proteins

2020

Abstract There are multiple definitions for low complexity regions (LCRs) in protein sequences, with all of them broadly considering LCRs as regions with fewer amino acid types compared to an average composition. Following this view, LCRs can also be defined as regions showing composition bias. In this critical review, we focus on the definition of sequence complexity of LCRs and their connection with structure. We present statistics and methodological approaches that measure low complexity (LC) and related sequence properties. Composition bias is often associated with LC and disorder, but repeats, while compositionally biased, might also induce ordered structures. We illustrate this dichot…

Protein ConformationComputer scienceReview ArticleComputational biologyMeasure (mathematics)Evolution MolecularLow complexity03 medical and health sciencesProtein DomainsAmino Acid Sequencestructure[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Databases ProteinMolecular Biology030304 developmental biologyStructure (mathematical logic)0303 health sciencesSequence[SCCO.NEUR]Cognitive science/Neurosciencecomposition bias030302 biochemistry & molecular biologyProteinsdisorderlow complexity regionsStructure and function[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]AlgorithmsInformation SystemsBriefings in Bioinformatics
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Flanking regions determine the structure of the poly-glutamine homo- repeat in huntingtin through mechanisms common among glutamine-rich human protei…

2020

International audience; The causative agent of Huntington's disease, the poly-Q homo-repeat in the N-terminal region of huntingtin (httex1), is flanked by a 17-residue-long fragment (N17) and a proline-rich region (PRR), which promote and inhibit the aggregation propensity of the protein, respectively, by poorly understood mechanisms. Based on experimental data obtained from site-specifically labeled NMR samples, we derived an ensemble model of httex1 that identified both flanking regions as opposing poly-Q secondary structure promoters. While N17 triggers helicity through a promiscuous hydrogen bond network involving the side chains of the first glutamines in the poly-Q tract, the PRR prom…

Repetitive Sequences Amino AcidHuntingtinAmino Acid Motifs[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics03 medical and health sciencesHuntington's diseaseStructural BiologyHuman proteome projectmedicineHumans[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyHuman proteinsProtein secondary structure[SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]030304 developmental biology[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]Huntingtin Protein0303 health sciencesChemistry030302 biochemistry & molecular biologyPromotermedicine.diseaseCell biologyIntrinsically Disordered ProteinsGlutamine[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsPolyglutamic Acid[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Low Complexity Region
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Low‐complexity detection for uplink massive MIMO SCMA systems

2020

Paid Open Access UNIT agreement

Low complexityComputer architectureComputer scienceMIMOTelecommunications linkElectrical and Electronic EngineeringVDP::Teknologi: 500::Informasjons- og kommunikasjonsteknologi: 550Computer Science ApplicationsIET Communications
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin

2021

Low complexity regions (LCRs) are very frequent in protein sequences, generally having a lower propensity to form structured domains and tending to be much less evolutionarily conserved than globular domains. Their higher abundance in eukaryotes and in species with more cellular types agrees with a growing number of reports on their function in protein interactions regulated by post-translational modifications. LCRs facilitate the increase of regulatory and network complexity required with the emergence of organisms with more complex tissue distribution and development. Although the low conservation and structural flexibility of LCRs complicate their study, evolutionary studies of proteins …

Protein Conformation alpha-Helical0301 basic medicineNetwork complexityHuntingtinintrinsically disordered regionsAmino Acid MotifsComputational biologyBiologyprotein interactionsArticlecompositionally biased regionsCatalysisProtein–protein interactionlcsh:ChemistryEvolution MolecularInorganic ChemistryLow complexity03 medical and health sciencesProtein DomainsProtein Interaction MappingAnimalsHumansp300-CBP Transcription FactorsAmino Acid SequenceProtein Interaction MapsHuntingtinTissue distributionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyHuntingtin Protein030102 biochemistry & molecular biologyOrganic ChemistryNuclear Proteinsp120 GTPase Activating ProteinGeneral MedicineMultiple modesSynapsinslow complexity regionsComputer Science ApplicationshomorepeatsMicroscopy Electron030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Sequence AlignmentFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization

2014

The carbonic anhydrase (CA; EC 4.2.1.1) superfamily is a class of ubiquitous metallo-enzymes that catalyse the reversible hydration of carbon dioxide. The ?-CA family, present in all metazoan clades, is a key enzyme involved in a wide range of physiological functions including pH regulation, respiration, photosynthesis, and biocalcification. This paper reviews the evolution of the ?-CA family, with an emphasis on metazoan ?-CA members involved in biocalcification. Phylogenetic analyses reveal a complex evolutionary history of ?-CAs, and suggest ?-CA was independently co-opted into a variety of skeleton forming roles (e.g. as a provider of HCO3? ions, a structural protein, a nucleation activ…

Biomineralizationα-Carbonic anhydraseRepetitive low complexity domains (RLCDs)MetazoaBiocalcification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/Biomaterials551α -Carbonic anhydraseMolecular evolutionAnimal Science and ZoologyLow complexity domains (LCDs)[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsEcology Evolution Behavior and SystematicsFrontiers in Zoology
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The Conservation of Low Complexity Regions in Bacterial Proteins Depends on the Pathogenicity of the Strain and Subcellular Location of the Protein

2021

Low complexity regions (LCRs) in proteins are characterized by amino acid frequencies that differ from the average. These regions evolve faster and tend to be less conserved between homologs than globular domains. They are not common in bacteria, as compared to their prevalence in eukaryotes. Studying their conservation could help provide hypotheses about their function. To obtain the appropriate evolutionary focus for this rapidly evolving feature, here we study the conservation of LCRs in bacterial strains and compare their high variability to the closeness of the strains. For this, we selected 20 taxonomically diverse bacterial species and obtained the completely sequenced proteomes of t…

Proteomics0301 basic medicinelcsh:QH426-470030106 microbiologyBiologyArticlecompositionally biased regionsEvolution MolecularLow complexity03 medical and health sciencesBacterial ProteinsSequence Analysis ProteinGeneticsExtracellularGenetics (clinical)chemistry.chemical_classificationBacteriaVirulenceStrain (chemistry)Computational Biologybiology.organism_classificationlow complexity regionsAmino acidhomorepeatslcsh:Genetics030104 developmental biologychemistryEvolutionary biologybacterial strainsProteomeorthologyBacterial outer membraneBacteriaFunction (biology)host–pathogen interactionsGenes
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Mollusc shellomes: Past, present and future.

2020

13 pages; International audience; In molluscs, the shell fabrication requires a large array of secreted macromolecules including proteins and polysaccharides. Some of them are occluded in the shell during mineralization process and constitute the shell repertoire. The protein moieties, also called shell proteomes or, more simply, 'shellomes', are nowadays analyzed via high-throughput approaches. These latter, applied so far on about thirty genera, have evidenced the huge diversity of shellomes from model to model. They also pinpoint the recurrent presence of functional domains of diverse natures. Shell proteins are not only involved in guiding the mineral deposition, but also in enzymatic a…

[SDE] Environmental SciencesProteomeLarge arrayCarbohydratesMacroevolutionEmergent propertyLow complexity03 medical and health sciencesStructural BiologyAnimal Shells[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ShellAnimalsBiomineralComplex systems biology[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsShellomicsComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesMineralsMatrixChemistry030302 biochemistry & molecular biologyMineral depositionEvolvability[SDV.BA.ZI]Life Sciences [q-bio]/Animal biology/Invertebrate ZoologyEvolutionary biologyMolluscaProteome[SDE]Environmental Sciences[SDV.BA.ZI] Life Sciences [q-bio]/Animal biology/Invertebrate ZoologyMolluscJournal of structural biology
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Morphology-based measurement of activation time in human atrial fibrillation

2003

The measurement of the activation time is crucial to allow the correct automatic analysis and classification of intracardiac electrograms recorded in the human atria during atrial fibrillation (AF). This study proposes a method which accounts for the morphology of bipolar signals. After ventricular artifact removal and activation wave recognition, the fiducial point of the activation wave was set at its local barycentre (LB). The method was tested on a set of 30 AF bipolar recordings of increasing complexity class; its performance was compared with that of the traditional methods of maximum peak (MP) or maximum slope (MS) estimation, taking the manual measurements performed by an expert car…

Artifact (error)medicine.medical_specialtyMaximum slopemedicine.diagnostic_testComputer scienceAtrial fibrillationMathematical morphologymedicine.diseaseLow complexityInternal medicineSettore ING-INF/06 - Bioingegneria Elettronica E InformaticamedicineCardiologyFiducial markerCardiology and Cardiovascular MedicineElectrocardiographyIntracardiac ElectrogramSoftwareBiomedical engineering
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Self-organization of repetitive spike patterns in developing neuronal networks in vitro

2010

The appearance of spontaneous correlated activity is a fundamental feature of developing neuronal networks in vivo and in vitro. To elucidate whether the ontogeny of correlated activity is paralleled by the appearance of specific spike patterns we used a template-matching algorithm to detect repetitive spike patterns in multi-electrode array recordings from cultures of dissociated mouse neocortical neurons between 6 and 15 days in vitro (div). These experiments demonstrated that the number of spiking neurons increased significantly between 6 and 15 div, while a significantly synchronized network activity appeared at 9 div and became the main discharge pattern in the subsequent div. Repetiti…

Low complexityNetwork patternElectrophysiologyGeneral NeuroscienceSpike (software development)Gradual increaseBiologyNeuroscienceIn vitroNetwork activityEuropean Journal of Neuroscience
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