Search results for "Protein secondary structure"

showing 8 items of 88 documents

Topology-Dependent Swichability of Peptide Secondary Structures in Bioconjugates with Complex Architectures

2013

Peptide sequences, which exhibit a reversible pH-responsive coil to α-helix secondary structure transition, are conjugated to polymer precursors to yield linear AB and graft ABA peptide-poly(ethylene oxide) conjugates. While the PEO B-block is comparable, the conjugates differ in topologies of the peptide bearing A-blocks. The influences of topology on the structure transitions in the peptide segments are investigated, comparing linear AB-bioconjugates with graft ABA-bioconjugates having multiple peptide segments combined in star or pom-pom topologies.

chemistry.chemical_classificationPolymers and PlasticsEthylene oxideOrganic ChemistryPeptidePolymerConjugated systemMicroscopy Atomic ForceTopologyCombinatorial chemistryProtein Structure SecondaryPolyethylene Glycolschemistry.chemical_compoundchemistryMaterials ChemistrySelf-assemblyPeptidesProtein secondary structureTopology (chemistry)ConjugateMacromolecular Rapid Communications
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Formation of covalent di-tyrosine dimers in recombinant α-synuclein

2015

Parkinson's disease is associated with fibril deposition in the diseased brain. Misfolding events of the intrinsically disordered synaptic protein α-synuclein are suggested to lead to the formation of transient oligomeric and cytotoxic species. The etiology of Parkinson's disease is further associated with mitochondrial dysfunction and formation of reactive oxygen species. Oxidative stress causes chemical modification of native α-synuclein, plausibly further influencing misfolding events. Here, we present evidence for the spontaneous formation of covalent di-tyrosine α-synuclein dimers in standard recombinant protein preparations, induced without extrinsic oxidative or nitrative agents. The…

chemistry.chemical_classificationReactive oxygen speciesParkinson's diseasealphasynucleinamyloids di-tyrosine dimers EOM Parkinson’s disease SAXSSAXSOxidative phosphorylationFibrilmedicine.disease_causeIndustrial and Manufacturing Engineeringchemistry.chemical_compoundα-synucleinMonomerchemistryBiochemistryCovalent bondmedicinedi-tyrosine dimersamyloidsTyrosineProtein secondary structureEOMOxidative stressResearch PaperIntrinsically Disordered Proteins
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Identification of the membrane penetrating domain of Vibrio cholerae cytolysin as a β-barrel structure

2005

Summary Vibrio cholerae cytolysin (VCC) is an oligomerizing pore-forming toxin that is related to cytolysins of many other Gram-negative organisms. VCC contains six cysteine residues, of which two were found to be present in free sulphydryl form. The positions of two intramolecular disulphide bonds were mapped, and one was shown to be essential for correct folding of protoxin. Mutations were created in which the two free cysteines were deleted, so that single cysteine substitution mutants could be generated for site-specific labelling. Employment of polarity-sensitive fluorophores identified amino acid side-chains that formed part of the pore-forming domain of VCC. The sequence commenced at…

chemistry.chemical_classificationStereochemistryBiologymedicine.disease_causeAntiparallel (biochemistry)MicrobiologyAmino acidBiochemistrychemistryVibrio choleraemedicineCytolysinLipid bilayerMolecular BiologyPeptide sequenceProtein secondary structureCysteineMolecular Microbiology
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Predicted secondary structure of hydroperoxide lyase from green bell pepper cloned in the yeast Yarrowia lipolytica

2010

International audience; Fatty acid hydroperoxide lyase (HPL) is a member of the cytochrome P450 family acting on fatty acid hydroperoxides in many organisms. The active green bell pepper HPL, cloned and expressed in the yeast Yarrowia lipolytica, was purified by immobilized metal-ion affinity chromatography (IMAC) in the presence of 2% of Triton X-100R. The secondary structure prediction by bioinformatics servers of HPL was realized by ANTHEPROT software, using the GOR, DPM and Predator methods. The theoretical results which are average values obtained from three different calculation methods showed 33% α-helix, 18% β-sheet, 7% turn and 42% coil. On the other hand, the secondary structure a…

chemistry.chemical_classificationYarrowia lipolyticaCircular dichroismChromatographybiologyProcess Chemistry and Technology[SDV]Life Sciences [q-bio]Circular dichroism spectroscopyBioengineeringYarrowiabiology.organism_classificationBiochemistryCatalysisYeastRandom coilHydroperoxide lyaseEnzymeAffinity chromatographyBiochemistrychemistrySecondary structureSpecific activityPredictionProtein secondary structure
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Conformation of dehydropentapeptides containing four achiral amino acid residues - controlling the role of L-valine.

2014

Structural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (ΔZPhe and ΔAla) and two glycines, as well as one chiral L-Val residue were performed using NMR spectroscopy. The key role of the L-Val residue in the generation of the secondary structure of peptides is discussed. The obtained results suggest that the strongest influence on the conformation of peptides arises from a valine residue inserted at the C-terminal position. The most ordered conformation was found for peptide Boc-Gly-ΔAla-Gly-ΔZPhe-Val-OMe (3), which adopts a right-handed helical conformation.

chemistry.chemical_classificationconformationdehydropeptideChemistryStereochemistryOrganic ChemistryPeptideNuclear magnetic resonance spectroscopydehydroalaninedehydrophenylalanineFull Research PaperNMRlcsh:QD241-441Residue (chemistry)chemistry.chemical_compoundChemistrylcsh:Organic chemistryDehydroalanineValinelcsh:QAmino acid residuelcsh:ScienceProtein secondary structureBeilstein journal of organic chemistry
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Sugar moiety has a direct influence on the secondary structure and properties of sturgeon gonadotropin

2009

Sugar moiety has a direct influence on the secondary structure and properties of sturgeon gonadotropin Sturgeon Acipenser güldenstädti Br. gonadotropic hormone (GTH) β-subunit (β-GTH) was selectively chemically deglycosylated (dg) by anhydrous hydrogen fluoride and trifluoromethane sulfonic acid. Two dgβ-GTH molecular forms retaining 35% (dgβ-GTH1) and 13% (dgβ-GTH2) of their initial carbohydrates were obtained. Investigation of the reassociated α-β hybrid dimers (recombinants) α-GTH+dgβ-GTH1 and α-GTH+dgβ-GTH2 showed that the immunoreactivity with antiserum raised against standard GTH dropped by 22.5%. Hybrid dimers were recognised by the standard GTH antibodies, which indicated that the s…

endocrine systemMultidisciplinaryGeneral interestmedicine.drug_classChemistrySciencesecondary structure of the α-βQdeglycosylationdimersturgeon gonadotropic hormoneSturgeonBiochemistrymedicineSugar moietyβ-subunitGonadotropinProtein secondary structurebiological functionProceedings of the Latvian Academy of Sciences. Section B. Natural, Exact, and Applied Sciences.
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The Interaction Mechanism of Intrinsically Disordered PP2A Inhibitor Proteins ARPP-16 and ARPP-19 With PP2A

2021

Protein phosphatase 2A (PP2A) activity is critical for maintaining normal physiological cellular functions. PP2A is inhibited by endogenous inhibitor proteins in several pathological conditions including cancer. A PP2A inhibitor protein, ARPP-19, has recently been connected to several human cancer types. Accordingly, the knowledge about ARPP-19—PP2A inhibition mechanism is crucial for the understanding the disease development and the therapeutic targeting of ARPP-19—PP2A. Here, we show the first structural characterization of ARPP-19, and its splice variant ARPP-16 using NMR spectroscopy, and SAXS. The results reveal that both ARPP proteins are intrinsically disordered but contain transient…

macromolecular substancesIntrinsically disordered proteinsBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistryenvironment and public healthProtein–protein interactionprotein-protein interaction03 medical and health sciences0302 clinical medicineNMR spectroscopyIDPSARPP-16Molecular BiosciencesARPP-19NMR-spektroskopialcsh:QH301-705.5Molecular BiologyProtein secondary structure030304 developmental biologyOriginal Researchsoluviestintä0303 health sciencesMicroscale thermophoresisChemistryAlternative splicingInhibitor proteinProtein phosphatase 2Nuclear magnetic resonance spectroscopySAXS3. Good healthPP2APP2A inhibitor proteinssyöpäsolutlcsh:Biology (General)Biophysicsintrinsically disordered proteinsproteiinit030217 neurology & neurosurgery
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Distinctive attributes for predicted secondary structures at terminal sequences of non-classically secreted proteins from proteobacteria

2008

Abstract C- and N-terminal sequences (64 amino acid residues each) of 89 non-classically secreted type I, type III and type IV proteins (Swiss-Prot/TrEMBL) from proteobacteria were transformed into predicted secondary structures. Multivariate analysis of variance (MANOVA) confirmed the significance of location (C- or N-termini) and secretion type as essential factors in respect of quantitative representations of structured (a-helices, b-strands) and unstructured (coils) elements. The profiles of secondary structures were transcripted using unequal property values for helices, strands and coils and corresponding numerical vectors (independent variables) were subjected to multiple discriminan…

terminal sequencesMultiple discriminant analysisGeneral Immunology and MicrobiologybiologyQH301-705.5General Neurosciencesecondary structureComputational biologyLinear discriminant analysisbiology.organism_classificationBioinformaticsdiscriminant analysisGeneral Biochemistry Genetics and Molecular BiologyCross-validationSecretory proteinDiscriminantprotein secretionSecretionProteobacteriaBiology (General)General Agricultural and Biological SciencesProtein secondary structureproteobacteriaOpen Life Sciences
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