Search results for "Peptide sequence"

showing 10 items of 330 documents

Structural analysis of Drosophila subobscura gypsy elements (gypsyDs)

1997

The study of gypsy elements in Drosophila subobscura (gypsyDs) indicated that they are transcriptionally active and mobile. From the comparative analysis of a complete gypsyDs element with the canonical gypsy sequence from D. melanogaster (gypsyDm) it can be deduced that while the whole structure is maintained, the gypsyDs ORF3 encodes a non-functional Env protein. The PCR amplification and sequencing of the ORF3 from different laboratory strains and H271 clones show that all gypsyDs sequences studied have frame-shifting mutations in this region. These results support that gypsyDs elements lack functional Env proteins and consequently they lack infective ability. In this way, it can be prop…

GeneticsbiologylawMelanogasterRetrotransposonDrosophila (subgenus)biology.organism_classificationPeptide sequenceEnv ProteinDrosophila subobscuraPolymerase chain reactionlaw.inventionSequence (medicine)
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Nucleotide sequence of rat invariant γ chain cDNA clone pLRγ34.3

1988

Geneticschemistry.chemical_compoundCdna cloningchemistryChain (algebraic topology)GeneticsNucleic acid sequenceBase sequenceInvariant (mathematics)BiologyPeptide sequenceDNANucleic Acids Research
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Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles.

1998

ABSTRACT Unlike those of the S and the L envelope proteins, the functional role of the related M protein in the life cycle of the hepatitis B virus (HBV) is less understood. We now demonstrate that a single N glycan, specific for M, is required for efficient secretion of M empty envelope particles. Moreover, this glycan mediates specific association of M with the chaperone calnexin. Conversely, the N glycan, common to all three envelope proteins, is involved neither in calnexin binding nor in subviral particle release. As proper folding and trafficking of M need the assistance of the chaperone, the glycan-dependent association of M with calnexin may thus play a crucial role in the assembly …

GlycanHepatitis B virusGlycosylationGlycosylationCalnexinImmunologyBiologymedicine.disease_causeMicrobiologychemistry.chemical_compoundCytosolN-linked glycosylationViral Envelope ProteinsVirologyCalnexinmedicineAnimalsSecretionPeptide sequenceHepatitis B virusBase SequenceCalcium-Binding ProteinsVirus-Cell Interactionscarbohydrates (lipids)BiochemistrychemistryOligodeoxyribonucleotidesInsect ScienceChaperone (protein)COS Cellsbiology.proteinMutagenesis Site-DirectedJournal of virology
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Identification of a positively evolving putative binding region with increased variability in posttranslational motifs in zonadhesin MAM domain 2.

2005

Positive selection has been shown to be pervasive in sex-related proteins of many metazoan taxa. However, we are only beginning to understand molecular evolutionary processes on the lineage to humans. To elucidate the evolution of proteins involved in human reproduction, we studied the sequence evolution of MAM domains of the sperm-ligand zonadhesin in respect to single amino acid sites, solvent accessibility, and posttranslational modification. GenBank-data were supplemented by new cDNA-sequences of a representative non-human primate panel. Solvent accessibility predictions identified a probably exposed fragment of 30 amino acids belonging to MAM domain 2 (i.e., MAM domain 3 in mouse). The…

GlycosylationGlycosylationMolecular Sequence DataBiologyProtein Serine-Threonine Kinaseschemistry.chemical_compoundMiceN-linked glycosylationGenetic variationGeneticsAnimalsAmino Acid SequenceBinding sitePhosphorylationSelection GeneticMolecular BiologyPeptide sequenceEcology Evolution Behavior and SystematicsBinding selectivitychemistry.chemical_classificationGeneticsBinding SitesBase SequenceSequence Homology Amino AcidGenetic VariationMembrane ProteinsAmino acidRepressor ProteinsSperm MaturationchemistryMultigene FamilyPhosphorylationProtein Processing Post-TranslationalTranscription FactorsMolecular phylogenetics and evolution
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Efficient expression of a Paenibacillus barcinonensis endoglucanase in Saccharomyces cerevisiae.

2011

Abstract The endoglucanase coded by celA (GenBank Access No. Y12512) from Paenibacillus barcinonensis, an enzyme with good characteristics for application on paper manufacture from agricultural fibers, was expressed in Saccharomyces cerevisiae by using different domains of the cell wall protein Pir4 as translational fusion partners, to achieve either secretion or cell wall retention of the recombinant enzyme. Given the presence of five potential N-glycosylation sites in the amino acid sequence coded by celA, the effect of glycosylation on the enzymatic activity of the recombinant enzyme was investigated by expressing the recombinant fusion proteins in both, standard and glycosylation-defici…

GlycosylationGlycosylationSaccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeBioengineeringCellulaseSaccharomyces cerevisiaeApplied Microbiology and Biotechnologylaw.inventionchemistry.chemical_compoundBacterial ProteinsCellulaselawPeptide sequencechemistry.chemical_classificationbiologybiology.organism_classificationFusion proteinYeastEnzymeBiochemistrychemistryBatch Cell Culture TechniquesRecombinant DNAbiology.proteinPaenibacillusBiotechnologyJournal of industrial microbiologybiotechnology
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A Cell-specific Glycosylated Silk Protein from Chironomus thummi Salivary Glands

1996

Chironomid salivary glands contain 40 cells dedicated to the synthesis of a relatively small ensemble of silk proteins. Glands in some species contain a special lobe composed of 4 cells distinguishable from the others. We have cloned a special lobe-specific cDNA from Chironomus thummi salivary glands. Northern blots of salivary gland RNA demonstrated that the cDNA hybridizes to a 2.5-kilobase transcript present only in the special lobe. In situ hybridization mapped the gene encoding this cDNA to region A2b on polytene chromosome IV, the locus of the special lobe-specific Balbiani ring a. The deduced amino acid sequence encodes a protein with a calculated molecular mass of 77 kDa and numerou…

GlycosylationPolytene chromosomeMolecular massSalivary glandCell BiologyBiologyBiochemistryMolecular biologyFusion proteinchemistry.chemical_compoundmedicine.anatomical_structurechemistryComplementary DNAmedicineMolecular BiologyPeptide sequenceGeneJournal of Biological Chemistry
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Membrane-insertion fragments of Bcl-xL, Bax, and Bid.

2004

Apoptosis regulators of the Bcl-2 family associate with intracellular membranes from mitochondria and the endoplasmic reticulum, where they perform their function. The activity of these proteins is related to the release of apoptogenic factors, sequestered in the mitochondria, to the cytoplasm, probably through the formation of ion and/or protein transport channels. Most of these proteins contain a C-terminal putative transmembrane (TM) fragment and a pair of hydrophobic alpha helices (alpha5-alpha6) similar to the membrane insertion fragments of the ion-channel domain of diphtheria toxin and colicins. Here, we report on the membrane-insertion properties of different segments from antiapopt…

GlycosylationStereochemistryRecombinant Fusion ProteinsMolecular Sequence Databcl-X ProteinBcl-xLApoptosisBiochemistryProtein Structure SecondaryMembrane LipidsMiceProtein structureBcl-2-associated X proteinPredictive Value of TestsProto-Oncogene ProteinsProtein Interaction MappingAnimalsHumansAmino Acid SequencePeptide sequencebcl-2-Associated X ProteinbiologyIntracellular MembranesTransmembrane proteinPeptide FragmentsTransport proteinProtein TransportProto-Oncogene Proteins c-bcl-2Multigene FamilyHelixbiology.proteinBiophysicsCarrier ProteinsHydrophobic and Hydrophilic InteractionsAlpha helixBH3 Interacting Domain Death Agonist ProteinBiochemistry
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Synthesis of Tn/T Antigen MUC1 Glycopeptide BSA Conjugates and Their Evaluation as Vaccines

2011

The tumor-associated mucin MUC1 over-expressed in most epithelial tumor tissues is considered a promising target for immunotherapy. The extracellular part of MUC1 contains a domain of numerous tandem repeats of the amino acid sequence HGVTSAPDTRPAPGSTAPPA, including five potential O-glycosylation sites. In this study, T9 and S15 have been chosen as the positions of glycosylation. The glycopeptides N-terminally equipped with a triethylene glycol spacer were synthesized by microwave-assisted Fmoc solid-phase peptide synthesis. After detachment from the resin and deprotection, the MUC1 glycopeptides were conjugated to bovine serum albumin (BSA). To evaluate the immunological properties, balb/c…

GlycosylationbiologyOrganic ChemistryGlycopeptidechemistry.chemical_compoundSolid-phase synthesischemistryBiochemistryAntigenPeptide synthesisbiology.proteinPhysical and Theoretical ChemistryBovine serum albuminPeptide sequenceMUC1European Journal of Organic Chemistry
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Maturation of barley cysteine endopeptidase expressed in Trichoderma reesei is distorted by incomplete processing

2002

Maturation of barley cysteine endopeptidase B (EPB) in Trichoderma reesei was studied with metabolic inhibitors, Western blotting, and immuno microscopy. The inactive 42-kDa recombinant EPB proprotein, first detected in apical cells, was sequentially processed in a time-dependent manner to a secreted polypeptide of 38.5 kDa, and thereafter, to polypeptides of 37.5, 35.5, and 32 kDa exhibiting enzyme activity both in the hyphae and culture medium. The sizes of the different forms of recombinant EPB were in accordance with molecular masses calculated from the deduced amino acid sequence, assuming cleavage at four putative Kex2p sites present in the 42-kDa proprotein. Both the liquid and the z…

GlycosylationglycosylationStereochemistryBlotting WesternMolecular Sequence DataImmunologyApplied Microbiology and BiotechnologyMicrobiologylaw.inventioncysteine proteinasemodified Golgi-like bodychemistry.chemical_compoundlawGeneticsAmino Acid SequenceProproteinMolecular BiologyPeptide sequenceTrichoderma reeseiGlycoproteinsTrichodermachemistry.chemical_classificationbiologyTunicamycinHordeumGeneral MedicineBrefeldin Abiology.organism_classificationKex2pRecombinant ProteinsEnzyme assayEnzyme ActivationMolecular WeightsecretionCysteine EndopeptidasesEnzymechemistryBiochemistryRecombinant DNAbiology.proteinProtein Processing Post-Translational
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Fine-mapping of the B-cell epitope domain at the N-terminus of the preS2 region of the hepatitis B surface antigen

2002

In this study, we report the exact localization and substitutional characterization of a B-cell epitope domain at the N-terminus of the preS2 region of the hepatitis B surface antigen. A set of deletion variants containing preS2 sequences of different length was generated on the basis of frCP as a carrier. It was found after Western blot analysis that three monoclonal antibodies (MAbs) (2-11B1, 3-11C2, HB.OT10) recognized the linear preS2 sequence within the amino acid (aa) stretch 3-WNSTTFHQTLQDP-13. The importance of each aa residue of the epitope was proved by comparison of antibody binding to alanine-substituted peptides in both free-peptide and Pepscan variants.

HBsAgmedicine.drug_classBlotting WesternMolecular Sequence DataImmunologyMonoclonal antibodyEpitopeMiceViral Envelope ProteinsmedicineAnimalsImmunology and AllergyAmino Acid SequenceProtein PrecursorsPeptide sequenceHepatitis B Surface AntigensLinear epitopebiologyAntibodies MonoclonalMolecular biologyEpitope mappingPepscanbiology.proteinEpitopes B-LymphocyteAntibodyEpitope MappingJournal of Immunological Methods
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