Search results for "Amino acid sequence"

showing 10 items of 1296 documents

Roles of a conserved proline in the internal fusion peptide of Ebola glycoprotein

2004

AbstractThe structural determinants underlying the functionality of viral internal fusion peptides (IFPs) are not well understood. We have compared EBOwt (GAAIGLAWIPYFGPAAE), representing the IFP of the Ebola fusion protein GP, and EBOmut (GAAIGLAWIPYFGRAAE) derived from a non-functional mutant with conserved Pro537 substituted by Arg. P537R substitution did not abrogate peptide-membrane association, but interfered with the ability to induce bilayer destabilization. Structural determinations suggest that Pro537 is required to preserve a membrane-perturbing local conformation in apolar environments.

Circular dichroismEbola glycoproteinProtein insertion into membranesProlinePeptide conformationMutantMolecular Sequence DataBiophysicsBiochemistrySendai viruschemistry.chemical_compoundStructural BiologyGeneticsProlineAmino Acid SequenceMolecular BiologyPeptide sequencePOPCchemistry.chemical_classificationChemistryProteïnes de membranaCell BiologyEbolavirusFusion proteinPeptide FragmentsPeptide ConformationViral fusion peptideBiochemistryAvian Sarcoma VirusesLiposomesHIV-1PèptidsGlycoproteinPeptide–lipid interactionViral Fusion ProteinsFEBS Letters
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Core Histones Are Glutaminyl Substrates for Tissue Transglutaminase

1996

Chicken erythrocyte core histones are glutaminyl substrates in the transglutaminase (TGase) reaction with monodansylcadaverine (DNC) as donor amine. The modification is very fast when compared with that of many native substrates of TGase. Out of the 18 glutamines of the four histones, nine (namely glutamine 95 of H2B; glutamines 5, 19, and 125 of H3; glutamines 27 and 93 of H4; and glutamines 24, 104, and 112 of H2A) are the amine acceptors in free histones. The use of Gln112 of H2A requires a temperature-dependent partial unfolding of the histone, showing that structural determinants are decisive for the glutamine specificity. The structures of H2A and H2B do not appreciably change upon mo…

Circular dichroismErythrocytesTissue transglutaminaseGlutamineGuinea PigsMolecular Sequence DataIn Vitro TechniquesBiochemistrySubstrate SpecificityHistoneschemistry.chemical_compoundCadaverineAnimalsNucleosomeAmino Acid SequenceMolecular BiologyPeptide sequenceTransglutaminasesMolecular StructurebiologyMethylamineCell BiologyNucleosomesChromatinGlutamineKineticsHistonechemistryBiochemistrybiology.proteinJournal of Biological Chemistry
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Characterization of the interaction between Actinin-Associated LIM Protein (ALP) and the rod domain of α-actinin

2009

Abstract Background The PDZ-LIM proteins are a family of signalling adaptors that interact with the actin cross-linking protein, α-actinin, via their PDZ domains or via internal regions between the PDZ and LIM domains. Three of the PDZ-LIM proteins have a conserved 26-residue ZM motif in the internal region, but the structure of the internal region is unknown. Results In this study, using circular dichroism and nuclear magnetic resonance (NMR), we showed that the ALP internal region (residues 107–273) was largely unfolded in solution, but was able to interact with the α-actinin rod domain in vitro, and to co-localize with α-actinin on stress fibres in vivo. NMR analysis revealed that the ti…

Circular dichroismPDZ domaineducationAmino Acid MotifsMolecular Sequence DataPlasma protein bindingActininmacromolecular substancesBiology03 medical and health sciences0302 clinical medicineCell Line TumorHumansActininAmino Acid Sequencelcsh:QH573-671Peptide sequenceActin030304 developmental biologyLIM domainFluorescent Dyes0303 health scienceslcsh:CytologyMicrofilament ProteinsCell BiologyLIM Domain ProteinsSurface Plasmon Resonancemusculoskeletal systemRecombinant ProteinsCell biologyProtein Structure TertiaryLHX3Peptides030217 neurology & neurosurgeryResearch ArticleProtein BindingBMC Cell Biology
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Novel atrazine-binding biomimetics inspired to the D1 protein from the photosystem II of Chlamydomonas reinhardtii.

2020

Biomimetic design represents an emerging field for improving knowledge of natural molecules, as well as to project novel artificial tools with specific functions for biosensing. Effective strategies have been exploited to design artificial bioreceptors, taking inspiration from complex supramolecular assemblies. Among them, size-minimization strategy sounds promising to provide bioreceptors with tuned sensitivity, stability, and selectivity, through the ad hoc manipulation of chemical species at the molecular scale. Herein, a novel biomimetic peptide enabling herbicide binding was designed bioinspired to the D1 protein of the Photosystem II of the green alga Chlamydomonas reinhardtii. The D1…

Circular dichroismPhotosystem IIProtein ConformationSupramolecular chemistryPlastoquinoneChlamydomonas reinhardtiiPeptide02 engineering and technologyMolecular Dynamics SimulationBiochemistryFluorescence spectroscopy03 medical and health scienceschemistry.chemical_compoundStructural BiologyBiomimeticsAmino Acid SequencePhotosynthesisMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyRational designphotosystem IIPhotosystem II Protein ComplexGeneral Medicine021001 nanoscience & nanotechnologybiology.organism_classificationSpectrometry FluorescencechemistryArtificial peptides Atrazine sensing Rational designBiophysicsThermodynamicsAtrazine0210 nano-technologyPeptidesChlamydomonas reinhardtiiInternational journal of biological macromolecules
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Environment- and sequence-dependent modulation of the double-stranded to single-stranded conformational transition of gramicidin A in membranes.

1998

The role of the membrane lipid composition and the individual Trp residues in the conformational rearrangement of gramicidin A along the folding pathway to its channel conformation has been examined in phospholipid bilayers by means of previously described size-exclusion high-performance liquid chromatography HPLC-based strategy (Bano et al. (1991) Biochemistry 30, 886). It has been demonstrated that the chemical composition of the membrane influences the transition rate of the peptide rearrangement from double-stranded dimers to beta-helical monomers. The chemical modification of Trp residues, or its substitution by the more hydrophobic residues phenylalanine or naphthylalanine, stabilized…

Circular dichroismStereochemistryProtein ConformationDimerPhenylalanineEnterococcus faeciumLipid BilayersMolecular Sequence DataPeptideMicrobial Sensitivity TestsBiochemistrychemistry.chemical_compoundProtein structureAmino Acid SequencePeptide sequenceChromatography High Pressure Liquidchemistry.chemical_classificationChemistryCholestenesCircular DichroismGramicidinTryptophanFolding (chemistry)MembraneSpectrometry FluorescenceAmino Acid SubstitutionGramicidinFatty Acids UnsaturatedPhosphatidylcholinesDimerizationBiochemistry
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Isolation and characterization of haemoporin, an abundant haemolymph protein from Aplysia californica.

2003

In the present study, we show the isolation and characterization of the protein haemoporin, which constitutes the second most abundant protein fraction in the haemolymph of the marine gastropod Aplysia californica. Although Aplysia is commonly used to investigate the molecular basis of learning, not much is known about the proteins in its haemolymph, which is in contact with the neurons owing to the open circulatory system of molluscs. In the native state, haemoporin is a macromolecular complex forming a cylinder with a central solvent-filled pore. The native complex most probably is a homopentamer made up from 70 kDa subunits with a molecular mass of 360 kDa and a sedimentation coefficient…

Circular dichroismanimal structuresMolecular Sequence DataMegathura crenulataBiochemistrySequence Analysis ProteinHemolymphHemolymphAplysiaNative stateAnimalsAmino Acid SequenceMolecular BiologyProtein secondary structurebiologyMolecular massCircular DichroismCell BiologyAnatomyBlood Proteinsbiology.organism_classificationMolecular WeightMicroscopy ElectronSpectrometry FluorescenceBiochemistryAplysiaProtein quaternary structureElectrophoresis Polyacrylamide GelUltracentrifugationResearch ArticleThe Biochemical journal
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Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase

1995

Processing of the hepatitis C virus polyprotein is accomplished by a series of cotranslational and posttranslational cleavages mediated by host cell signalases and two virally encoded proteinases. Of these the NS3 proteinase is essential for processing at the NS3/4A, NS4A/4B, NS4B/5A, and NS5A/5B junctions. Processing between NS3 and NS4A occurs in cis, implying an intramolecular reaction mechanism, whereas cleavage at the other sites can also be mediated in trans. Sequence analysis of the amino termini of mature cleavage products and comparisons of amino acid residues around the scissile bonds of various hepatitis C virus isolates identified amino acid residues which might contribute to su…

Cleavage factorvirusesMolecular Sequence DataImmunologyHepacivirusCleavage and polyadenylation specificity factorViral Nonstructural ProteinsBiologyCleavage (embryo)MicrobiologySubstrate SpecificityScissile bondVirologyHumansAmino Acid SequenceAmino AcidsPeptide sequencechemistry.chemical_classificationNS3Cleavage stimulation factorHydrolysisSerine Endopeptidasesbiochemical phenomena metabolism and nutritionAmino acidchemistryBiochemistryMutagenesisInsect ScienceProtein Processing Post-TranslationalRNA HelicasesHeLa CellsResearch ArticleJournal of Virology
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Sequencing and analysis of the gene encoding the α-toxin of Clostridium novyi proves its homology to toxins A and B of Clostridium difficile

1995

A library of total Clostridium novyi DNA was established and screened for the alpha-toxin gene (tcn alpha) by hybridization with oligonucleotides derived from a partial N-terminal sequence and by using specific antisera. Overlapping subgenic tcn alpha fragments were isolated and subsequently the total sequence of tcn alpha was determined. The 6534 nucleotide open reading frame encodes a polypeptide of M(r) 250,166 and pI 5.9. The N-terminal alpha-toxin (Tcn alpha) sequence MLITREQLMKIASIP determined by Edman degradation confirmed the identity of the reading frame and the assignment of the translation start point. The toxin is not modified posttranslationally at its N-terminus nor does it co…

ClostridiumGenomic LibraryBase SequenceSequence Homology Amino AcidbiologyEdman degradationClostridioides difficileOligonucleotideBacterial ToxinsMolecular Sequence DataClostridium difficileClostridium novyibiology.organism_classificationRecombinant ProteinsHomology (biology)EnterotoxinsOpen reading frameBacterial ProteinsBiochemistryType C PhospholipasesGeneticsAmino Acid SequenceMolecular BiologyGenePeptide sequenceMolecular and General Genetics MGG
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Novel form of X-linked nonsyndromic hearing loss with cochlear malformation caused by a mutation in the type IV collagen gene COL4A6

2013

Hereditary hearing loss is the most common human sensorineural disorder. Genetic causes are highly heterogeneous, with mutations detected in >40 genes associated with nonsyndromic hearing loss, to date. Whereas autosomal recessive and autosomal dominant inheritance is prevalent, X-linked forms of nonsyndromic hearing impairment are extremely rare. Here, we present a Hungarian three-generation family with X-linked nonsyndromic congenital hearing loss and the underlying genetic defect. Next-generation sequencing and subsequent segregation analysis detected a missense mutation (c.1771G>A, p.Gly591Ser) in the type IV collagen gene COL4A6 in all affected family members. Bioinformatic analysis an…

Collagen Type IVMaleHearing lossDNA Mutational AnalysisMolecular Sequence DataMutation MissenseGene ExpressionDeafnessBiologyCongenital hearing lossmedicine.disease_causeArticleType IV collagenotorhinolaryngologic diseasesGeneticsmedicineAnimalsHumansMissense mutationGenetic Predisposition to DiseaseAmino Acid SequenceAlport syndromeGeneCells CulturedGenetic Association StudiesZebrafishGenetics (clinical)GeneticsMutationGenetic Diseases X-LinkedMiddle Agedmedicine.diseaseCochleaPedigreeMice Inbred C57BLChild PreschoolFemaleRNA Splice SitesOtic vesiclemedicine.symptomEuropean Journal of Human Genetics
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Characterization of a Novel Type of Serine/Threonine Kinase That Specifically Phosphorylates the Human Goodpasture Antigen

1999

Goodpasture disease is an autoimmune disorder that occurs naturally only in humans. Also exclusive to humans is the phosphorylation process that targets the unique N-terminal region of the Goodpasture antigen. Here we report the molecular cloning of GPBP (Goodpasture antigen-binding protein), a previously unknown 624-residue polypeptide. Although the predicted sequence does not meet the conventional structural requirements for a protein kinase, its recombinant counterpart specifically binds to and phosphorylates the exclusive N-terminal region of the human Goodpasture antigen in vitro. This novel kinase is widely expressed in human tissues but shows preferential expression in the histologic…

Collagen Type IVMolecular Sequence DataSaccharomyces cerevisiaeProtein Serine-Threonine KinasesMolecular cloningBiologymedicine.disease_causeAutoantigensBiochemistryCell LineAutoimmunitymedicineHumansAmino Acid SequenceCloning MolecularPhosphorylationMolecular BiologyPeptide sequenceCeramide Transfer ProteinSerine/threonine-specific protein kinaseBase SequenceSequence Homology Amino AcidKinaseCell BiologyCeramide transportImmunohistochemistryCell biologyBiochemistryProtein BiosynthesisPhosphorylationCollagenJournal of Biological Chemistry
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