Search results for "SECONDARY STRUCTURE"

showing 10 items of 106 documents

The effect of RNA substitution models on viroid and RNA virus phylogenies.

2018

Abstract Many viroids and RNA viruses have genomes that exhibit secondary structure, with paired nucleotides forming stems and loops. Such structures violate a key assumption of most methods of phylogenetic reconstruction, that sequence change is independent among sites. However, phylogenetic analyses of these transmissible agents rarely use evolutionary models that account for RNA secondary structure. Here, we assess the effect of using RNA-specific nucleotide substitution models on the phylogenetic inference of viroids and RNA viruses. We obtained data sets comprising full-genome nucleotide sequences from six viroid and ten single-stranded RNA virus species. For each alignment, we inferre…

0106 biological sciences0301 basic medicineRNA virusViroidvirusesComputational biologyBiology010603 evolutionary biology01 natural sciencesNucleic acid secondary structure03 medical and health scienceschemistry.chemical_compoundPhylogeneticsGeneticsRNA VirusesEcology Evolution Behavior and SystematicsPhylogenyPhylogenetic treeModels GeneticviroidModel selectionRNARNA virusbiology.organism_classificationRNA secondary structureViroidsphylogenetics030104 developmental biologychemistryDNAResearch Article
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SHAPE MATTERS: EFFECT OF POINT MUTATIONS ON RNA SECONDARY STRUCTURE

2013

A suitable model to dive into the properties of genotype-phenotype landscapes is the relationship between RNA sequences and their corresponding minimum free energy secondary structures. Relevant issues related to molecular evolvability and robustness to mutations have been studied in this framework. Here, we analyze the one-mutant neighborhood of the predicted secondary structure of 46 different RNAs, including tRNAs, viroids, larger molecules such as Hepatitis-δ virus, and several random sequences. The probability distribution of the effect of point mutations in linear structural motifs of the secondary structure is well fit by Pareto or Lognormal probability distributions functions, indep…

0106 biological sciencesGenetics0303 health sciencesPoint mutationRNARobustness (evolution)Computational biologyBiology010603 evolutionary biology01 natural sciencesNucleic acid secondary structureEvolvability03 medical and health sciencesControl and Systems EngineeringProbability distributionStructural motifRNA secondary structure sequence-structure map mutational effects linear motifsProtein secondary structure030304 developmental biologyAdvances in Complex Systems
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Secondary structure and dynamics study of the intrinsically disordered silica-mineralizing peptide P5S3during silicic acid condensation and silica de…

2017

The silica forming repeat R5 of sil1 from Cylindrotheca fusiformis was the blueprint for the design of P5 S3 , a 50-residue peptide which can be produced in large amounts by recombinant bacterial expression. It contains 5 protein kinase A target sites and is highly cationic due to 10 lysine and 10 arginine residues. In the presence of supersaturated orthosilicic acid P5 S3 enhances silica-formation whereas it retards the dissolution of amorphous silica (SiO2 ) at globally undersaturated concentrations. The secondary structure of P5 S3 during these 2 processes was studied by circular dichroism (CD) spectroscopy, complemented by nuclear magnetic resonance (NMR) spectroscopy of the peptide in …

0301 basic medicineCircular dichroismProtein ConformationSilicic AcidPeptideMolecular Dynamics SimulationSodium Chloride010402 general chemistry01 natural sciencesBiochemistryArticle03 medical and health scienceschemistry.chemical_compoundStructural BiologyPolymer chemistryOrganic chemistrySilicic acidNuclear Magnetic Resonance BiomolecularMolecular BiologyDissolutionProtein secondary structurePolyproline helixchemistry.chemical_classificationNuclear magnetic resonance spectroscopySilicon Dioxide0104 chemical sciencesIntrinsically Disordered Proteins030104 developmental biologychemistryPolymerizationPeptidesProteins: Structure, Function, and Bioinformatics
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Effect of high pressure on the antimicrobial activity and secondary structure of the bacteriocin nisin

2018

International audience; Effect of high pressure (HP) treatment on the antimicrobial properties and the structure of nisin was evaluated. Nisin solutions at pH 2.8 or 6.1 were treated by HP at 500 MPa – 10 min – 20 °C and their antimicrobial potency was determined. It appeared that HP clearly impacted the antimicrobial activity of nisin, with respective activity loss of 22.5% and 49.9% at pH 2.8 and 6.1. Structural analysis of nisin by circular dichroism and Fourier transform-infrared spectroscopies revealed that the decrease of nisin antimicrobial activity was likely due to the unfolding of the protein induced by HP. A loss of nisin β-turns structure, particularly significant at neutral pH,…

0301 basic medicineCircular dichroismfood.ingredient030106 microbiologyIndustrial and Manufacturing Engineering03 medical and health scienceschemistry.chemical_compound0404 agricultural biotechnologyfoodBacteriocinSecondary structure[SDV.IDA]Life Sciences [q-bio]/Food engineeringpolycyclic compoundsPotencyFood scienceProtein secondary structureNisinNisinbiologyFood additive[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringfood and beverages04 agricultural and veterinary sciencesGeneral Chemistrybiochemical phenomena metabolism and nutritionAntimicrobialbiology.organism_classification040401 food scienceActivityHigh pressurechemistrybacterialipids (amino acids peptides and proteins)BacteriaFood Science
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Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages.

2016

We are thankful to the MAX-lab staff for their support during our visit at the synchrotron.; International audience; AP205 is a single-stranded RNA bacteriophage that has a coat protein sequence not similar to any other known single-stranded RNA phage. Here, we report an atomic-resolution model of the AP205 virus-like particle based on a crystal structure of an unassembled coat protein dimer and a cryo-electron microscopy reconstruction of the assembled particle, together with secondary structure information from site-specific solid-state NMR data. The AP205 coat protein dimer adopts the conserved Leviviridae coat protein fold except for the N-terminal region, which forms a beta-hairpin in …

0301 basic medicineModels MolecularRNA bacteriophageViral proteinCryo-electron microscopyProtein Conformation010402 general chemistrymedicine.disease_causeCrystallography X-Ray01 natural sciencesvirus-like particleBacteriophage03 medical and health sciencesStructural Biology[CHIM.ANAL]Chemical Sciences/Analytical chemistryLeviviridaemedicineRNA VirusesBacteriophages[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyProtein secondary structurebiologyCryoelectron MicroscopyRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologycircular permutationRNA PhagesCircular permutation in proteinsbiology.organism_classification3. Good health0104 chemical sciencesCrystallography030104 developmental biologycoat proteinBiophysicsLeviviridaeCapsid ProteinsJournal of molecular biology
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2017

Proteins containing glutamine repeats (polyQ) are known to be structurally unstable. Abnormal expansion of polyQ in some proteins exceeding a certain threshold leads to neurodegenerative disease, a symptom of which are protein aggregates. This has led to extensive research of the structure of polyQ stretches. However, the accumulation of contradictory results suggests that protein context might be of importance. Here we aimed to evaluate the structural context of polyQ regions in proteins by analysing the secondary structure of polyQ proteins and their homologs. The results revealed that the secondary structure in polyQ vicinity is predominantly random coil or helix. Importantly, the region…

0301 basic medicineMultidisciplinary030102 biochemistry & molecular biologybiologyChemistrySaccharomyces cerevisiaeStructural contextContext (language use)Protein aggregationbiology.organism_classificationRandom coilProtein–protein interactionCell biology03 medical and health sciences030104 developmental biologyProtein structureProtein secondary structurePLOS ONE
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Parsimonious Scenario for the Emergence of Viroid-Like Replicons De Novo

2019

This article belongs to the Special Issue Viroid-2018: International Conference on Viroids and Viroid-Like RNAs. Viroids are small, non-coding, circular RNA molecules that infect plants. Different hypotheses for their evolutionary origin have been put forward, such as an early emergence in a precellular RNA World or several de novo independent evolutionary origins in plants. Here, we discuss the plausibility of de novo emergence of viroid-like replicons by giving theoretical support to the likelihood of different steps along a parsimonious evolutionary pathway. While Avsunviroidae-like structures are relatively easy to obtain through evolution of a population of random RNA sequences of fixe…

0301 basic medicinePopulation dynamicsViroidMatemáticasvirusesPopulationPospiviroidaelcsh:QR1-502Computational biologycomputational simulationsVirus Replicationlcsh:MicrobiologyArticleNucleic acid secondary structureEvolution MolecularViral Proteins03 medical and health sciences0302 clinical medicineCircular RNAVirologypopulation dynamicsModular evolutionRepliconeducationPolymeraseBiología y BiomedicinaSimple replicatorsComputational simulationseducation.field_of_studyViroidstructure enumerationbiologysimple replicatorsviroidStructure enumerationRNARNA Circularbiology.organism_classificationRNA secondary structureViroids030104 developmental biologyInfectious Diseasesbiology.proteinNucleic Acid ConformationRNA ViralRepliconmodular evolution030217 neurology & neurosurgeryViruses
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Insights into the Structure of the Vip3Aa Insecticidal Protein by Protease Digestion Analysis

2017

Vip3 proteins are secretable proteins from Bacillus thuringiensis whose mode of action is still poorly understood. In this study, the activation process for Vip3 proteins was closely examined in order to better understand the Vip3Aa protein stability and to shed light on its structure. The Vip3Aa protoxin (of 89 kDa) was treated with trypsin at concentrations from 1:100 to 120:100 (trypsin:Vip3A, w:w). If the action of trypsin was not properly neutralized, the results of SDS-PAGE analysis (as well as those with Agrotis ipsilon midgut juice) equivocally indicated that the protoxin could be completely processed. However, when the proteolytic reaction was efficiently stopped, it was revealed t…

0301 basic medicineProteasesHealth Toxicology and MutagenesisSize-exclusion chromatographyBeta sheetBacillus thuringiensislcsh:MedicineBiologyToxicologyCleavage (embryo)ArticleProtein Structure Secondary03 medical and health sciencestrypsin inhibitorsBacterial ProteinsSDS-PAGE artefactprotease stabilitymedicinebacterial secreted proteinsAnimalsTrypsinMode of actionProtein secondary structureVip proteinsIntestinal Secretionslcsh:Rtoxin activationVip proteins; bacterial secreted proteins; toxin activation; proteolytic activation; trypsin inhibitors; <i>Bacillus thuringiensis</i>; SDS-PAGE artefact; protease stabilityTrypsinMolecular biologyLepidoptera030104 developmental biologyBiochemistryproteolytic activationLarvaProteolysisPeptidesAlpha helixmedicine.drugToxins
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The C-terminal region of human plasma fetuin-B is dispensable for the raised-elephant-trunk mechanism of inhibition of astacin metallopeptidases

2019

© The Author(s) 2019.

0301 basic medicineProteasesProtein Conformationlcsh:MedicineAstacoideaCrystallography X-RayCleavage (embryo)Protein Structure SecondaryArticleMice03 medical and health sciencesScissile bondHydrolaseAnimalsHumansAmino Acid Sequencelcsh:ScienceProtein secondary structureX-ray crystallographyBinding SitesMultidisciplinary030102 biochemistry & molecular biologyChemistrylcsh:RMetalloendopeptidasesProteasesFetuinFetuin-BCell biologyZincFertility030104 developmental biologyProteolysisMetalloproteaseslcsh:QAstacinLinkerScientific Reports
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Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions.

2016

Lunasin is a 43 amino acid peptide with anti-cancer, antioxidant, anti-inflammatory and cholesterol-lowering properties. Although the mechanism of action of lunasin has been characterized to some extent, its exact three-dimensional structure as well as the function of the N-terminal sequence remains unknown. We established a novel method for the production of recombinant lunasin that allows efficient isotope labeling for NMR studies. Initial studies showed that lunasin can exist in a reduced or oxidized state with an intramolecular disulfide bond depending on solution conditions. The structure of both forms of the peptide at pH 3.5 and 6.5 was characterized by CD spectroscopy and multidimen…

0301 basic medicineProtein Conformation alpha-HelicalCircular dichroismPhysiologyBeta sheetPeptideIntrinsically disordered proteinsBiochemistryLunasinAntioxidantsHistones03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineEndocrinologyNeoplasmsAnticarcinogenic AgentsHumansAmino Acid SequenceDisulfidesProtein secondary structureNuclear Magnetic Resonance BiomolecularPlant Proteinschemistry.chemical_classificationChemistryAcetylationNuclear magnetic resonance spectroscopyIntrinsically Disordered Proteins030104 developmental biologyBiochemistry030220 oncology & carcinogenesisBiophysicsSoybean ProteinsPeptidesOxidation-ReductionFunction (biology)Peptides
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