Search results for "Protein structure"

showing 10 items of 757 documents

Polar/Ionizable Residues in Transmembrane Segments: Effects on Helix-Helix Packing

2012

The vast majority of membrane proteins are anchored to biological membranes through hydrophobic alpha-helices. Sequence analysis of high-resolution membrane protein structures show that ionizable amino acid residues are present in transmembrane (TM) helices, often with a functional and/or structural role. Here, using as scaffold the hydrophobic TM domain of the model membrane protein glycophorin A (GpA), we address the consequences of replacing specific residues by ionizable amino acids on TM helix insertion and packing, both in detergent micelles and in biological membranes. Our findings demonstrate that ionizable residues are stably inserted in hydrophobic environments, and tolerated in t…

Protein Foldinglcsh:MedicineBiochemistryBiotecnologiaProtein Structure SecondaryCell membraneGlycophorinsAmino Acidslcsh:ScienceMicelleschemistry.chemical_classificationMultidisciplinarybiologySodium Dodecyl SulfateLipidsTransmembrane proteinAmino acidmedicine.anatomical_structureBiochemistryCytochemistryThermodynamicsResearch ArticleProtein StructureBiophysicsCalcium-Transporting ATPasesProtein ChemistryProtein–protein interactionMembranes (Biologia)MicrosomesEscherichia colimedicineGlycophorinProtein InteractionsBiologyCell Membranelcsh:RMembrane ProteinsProteinsComputational BiologyBiological membraneIntracellular MembranesProtein Structure TertiaryTransmembrane ProteinsMembrane proteinchemistryHelixbiology.proteinBiophysicslcsh:QProtein Multimerization
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A Membrane-Bound Vertebrate Globin

2011

The family of vertebrate globins includes hemoglobin, myoglobin, and other O(2)-binding proteins of yet unclear functions. Among these, globin X is restricted to fish and amphibians. Zebrafish (Danio rerio) globin X is expressed at low levels in neurons of the central nervous system and appears to be associated with the sensory system. The protein harbors a unique N-terminal extension with putative N-myristoylation and S-palmitoylation sites, suggesting membrane-association. Intracellular localization and transport of globin X was studied in 3T3 cells employing green fluorescence protein fusion constructs. Both myristoylation and palmitoylation sites are required for correct targeting and m…

Protein StructureLipoylationGreen Fluorescent ProteinsMolecular Sequence Datalcsh:MedicineHemeBiochemistryCell membranechemistry.chemical_compoundModel OrganismsPalmitoylationhemic and lymphatic diseasesmedicineAnimalsRespiratory functionAmino Acid SequenceGlobinlcsh:ScienceProtein InteractionsBiologyZebrafishZebrafishMyristoylationHemoproteinsMultidisciplinarySequence Homology Amino Acidbiologylcsh:RCell MembraneMembrane ProteinsProteinsGene Expression Regulation DevelopmentalAnimal Modelsbiology.organism_classificationRecombinant ProteinsGlobinsGlobin foldOxygenmedicine.anatomical_structureBiochemistryMyoglobinchemistryImmunoglobulin GCytochemistrylcsh:QRabbitsResearch ArticleSubcellular FractionsPLoS ONE
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Thioflavin T templates amyloid β(1–40) conformation and aggregation pathway

2015

Aβ(1-40) peptide supramolecular assembly and fibril formation processes are widely recognized to have direct implications in the progression of Alzheimer's disease. The molecular basis of this biological process is still unknown and there is a strong need of developing effective strategies to control the occurring events. To this purpose the exploitation of small molecules interacting with Aβ aggregation represents one of the possible routes. Moreover, the use specific labeling has represented so far one of the most common and effective methods to investigate such a process. This possibility in turn rests on the reliability of the probe/labels involved. Here we present evidences of the effe…

Protein StructureSecondaryAβ(1–40) peptideAmyloidProtein ConformationMolecular Sequence DataBiophysicsSupramolecular chemistryMolecular Dynamics SimulationProtein aggregationProtein Aggregation PathologicalBiochemistryProtein Structure SecondarySupramolecular assemblyProtein Aggregateschemistry.chemical_compoundProtein structureAlzheimer DiseasePathologicalSecondary structureAβ(1-40) peptideHumansBenzothiazolesAmino Acid SequenceFluorescent DyesAmyloid beta-PeptidesProtein StabilityOrganic ChemistryAlzheimer's diseaseProtein AggregationSmall moleculePeptide FragmentsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Peptide ConformationAlzheimer's disease; Aβ(1–40) peptide; Protein aggregation; Protein conformation; Secondary structure; Thioflavin T; Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Fluorescence Recovery After Photobleaching; Fluorescent Dyes; Humans; Molecular Dynamics Simulation; Molecular Sequence Data; Peptide Fragments; Protein Aggregates; Protein Aggregation Pathological; Protein Conformation; Protein Multimerization; Protein Stability; Protein Structure Secondary; ThiazolesThiazolesBiophysicBiochemistrychemistryThioflavin TBiophysicsThioflavinProtein MultimerizationFluorescence Recovery After PhotobleachingBiophysical Chemistry
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Mutational analyses of YqjA, a Tvp38/DedA protein of E. coli

2015

AbstractMembrane proteins of the DedA/Tvp38 protein family are involved in membrane integrity and virulence of pathogenic organisms. However, the structure and exact function of any member of this large protein family are still unclear. In the present study we analyzed the functional and structural properties of a DedA homolog. Purified YqjA variants from Escherichia coli are detectable in different oligomeric states and specific homo-interaction of YqjA monomers in the membrane were confirmed by formation of a disulfide bond in the C-terminal transmembrane helix. Moreover, alanine scanning mutagenesis exhibited different interaction sites crucial for YqjA activity vs. dimer formation.

Protein familyDNA Mutational AnalysisBiophysicsVirulencelac operonmedicine.disease_causeBiochemistryProtein Structure SecondaryTvp38Structural BiologyEscherichia coliGeneticsmedicineOligomerizationFunctionMolecular BiologyEscherichia coliAlanineChemistryEscherichia coli ProteinsCell MembraneMutagenesisMembrane ProteinsGene Expression Regulation BacterialCell BiologyAlanine scanningTransmembrane domainMembrane proteinBiochemistryDedAMembrane proteinMutationProtein MultimerizationFEBS Letters
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Identification of new claudin family members by a novel PSI-BLAST based approach with enhanced specificity.

2006

In an attempt to develop a novel strategy for the identification of new members of protein families by in silico approaches, we have developed a semi-automated procedure of consecutive PSI-BLAST (Position-Specific-Iterated Basic Local Alignment Search Tool) searches incorporating identificiation as well as subsequent validation of putative candidates. For a proof of concept study we chose the search for novel members of the claudin family. The initial step was an iterated PSI-BLAST search starting with the PMP22_Claudin domain of each known member of the claudin family against the human part of the RefSeq Database. Putative new claudin domains derived from the converged list were evaluated …

Protein familyIn silicoMolecular Sequence DataSequence alignmentBiologycomputer.software_genreBiochemistrySet (abstract data type)Protein structureStructural BiologySequence Analysis ProteinRefSeqFalse positive paradoxHumansAmino Acid SequenceClaudinDatabases ProteinMolecular BiologyPhylogenyReverse Transcriptase Polymerase Chain ReactionComputational BiologyMembrane ProteinsProtein Structure TertiaryData miningcomputerSequence AlignmentProteins
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Bioinformatic flowchart and database to investigate the origins and diversity of Clan AA peptidases

2009

Abstract Background Clan AA of aspartic peptidases relates the family of pepsin monomers evolutionarily with all dimeric peptidases encoded by eukaryotic LTR retroelements. Recent findings describing various pools of single-domain nonviral host peptidases, in prokaryotes and eukaryotes, indicate that the diversity of clan AA is larger than previously thought. The ensuing approach to investigate this enzyme group is by studying its phylogeny. However, clan AA is a difficult case to study due to the low similarity and different rates of evolution. This work is an ongoing attempt to investigate the different clan AA families to understand the cause of their diversity. Results In this paper, we…

Protein familySequence analysisImmunologyProtein domainMolecular Sequence DataBiologycomputer.software_genreGeneral Biochemistry Genetics and Molecular BiologyProtein Structure SecondaryPhylogeneticsSequence Analysis ProteinSoftware DesignConsensus SequenceConsensus sequenceAspartic Acid EndopeptidasesClanAmino Acid SequenceDatabases ProteinPeptide sequencelcsh:QH301-705.5Ecology Evolution Behavior and SystematicsPhylogenyDatabaseAgricultural and Biological Sciences(all)Biochemistry Genetics and Molecular Biology(all)Applied MathematicsResearchComputational BiologyGenetic VariationGene AnnotationTemplates GeneticMarkov ChainsProtein Structure Tertiarylcsh:Biology (General)Modeling and SimulationGeneral Agricultural and Biological SciencescomputerBiology Direct
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A novel approach to investigate the evolution of structured tandem repeat protein families by exon duplication.

2020

Tandem Repeat Proteins (TRPs) are ubiquitous in cells and are enriched in eukaryotes. They contributed to the evolution of organism complexity, specializing for functions that require quick adaptability such as immunity-related functions. To investigate the hypothesis of repeat protein evolution through exon duplication and rearrangement, we designed a tool to analyze the relationships between exon/intron patterns and structural symmetries. The tool allows comparison of the structure fragments as defined by exon/intron boundaries from Ensembl against the structural element repetitions from RepeatsDB. The all-against-all pairwise structural alignment between fragments and comparison of the t…

Protein familyStructural alignmentBiological data visualizationExonComputational biologyBiologyEvolution Molecular03 medical and health sciencesExonProtein structureTandem repeatStructural BiologyGene duplicationAnimalsHumans030304 developmental biology0303 health sciences030302 biochemistry & molecular biologyIntronProteinsExonsProtein superfamilyClassificationIntronsBiological data visualization; Classification; Exon; Protein evolution; Protein structure; Repeat proteinTandem Repeat SequencesRepeat proteinProtein structureProtein evolutionJournal of structural biology
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RepeatsDB

2015

Database of annotated tandem repeat protein structures.

Protein structure analysisSequence composition complexity and repeats
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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
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A computer system to perform structure comparison using TOPS representations of protein structure

2001

We describe the design and implementation of a fast topology-based method for protein structure comparison. The approach uses the TOPS topological representation of protein structure, aligning two structures using a common discovered pattern and generating measure of distance derived from an insert score. Heavy use is made of a constraint-based pattern-matching algorithm for TOPS diagrams that we have designed and described elsewhere (Bioinformatics 15(4) (1999) 317). The comparison system is maintained at the European Bioinformatics Institute and is available over the Web at tops.ebi.ac.uk/tops. Users submit a structure description in Protein Data Bank (PDB) format and can compare it with …

Protein structure databaseMeasure (data warehouse)Molecular StructureComputer scienceGeneral Chemical EngineeringProteinsSequence Homologycomputer.file_formatTOPSProtein structure predictioncomputer.software_genreProtein Data BankApplied Microbiology and BiotechnologyPattern Recognition AutomatedArtificial IntelligencePattern matchingData miningProtein topologyRepresentation (mathematics)computerAlgorithmsSoftwareBiotechnology
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