Search results for "Helix"

showing 10 items of 196 documents

2020

Teraryl-based alpha-helix mimetics have resulted in efficient inhibitors of protein-protein interactions (PPIs). Extending the concept to even longer oligoarene systems would allow for the mimicking of even larger interaction sites. We present a highly efficient synthetic modular access to quateraryl alpha-helix mimetics, in which, at first, two phenols undergo electrooxidative dehydrogenative cross-coupling. The resulting 4,4′-biphenol is then activated by conversion to nonaflates, which serve as leaving groups for iterative Pd-catalyzed Suzuki-cross-coupling reactions with suitably substituted pyridine boronic acids. This work, for the first time, demonstrates the synthetic efficiency of …

010405 organic chemistryPeptidomimetic010402 general chemistryElectrosynthesis01 natural sciencesCombinatorial chemistryCatalysis0104 chemical sciencesProtein–protein interactionCatalysischemistry.chemical_compoundchemistryPyridinePhenolsPhysical and Theoretical ChemistryTrifluoromethanesulfonateAlpha helixCatalysts
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Determining Factors for the Unfolding Pathway of Peptides, Peptoids, and Peptidic Foldamers.

2016

We present a study of the mechanical unfolding pathway of five different oligomers (α-peptide, β-peptide, δ-aromatic-peptides, α/γ-peptides, and β-peptoids), adopting stable helix conformations. Using force-probe molecular dynamics, we identify the determining structural factors for the unfolding pathways and reveal the interplay between the hydrogen bond strength and the backbone rigidity in the stabilization of their helix conformations. On the basis of their behavior, we classify the oligomers in four groups and deduce a set of rules for the prediction of the unfolding pathways of small foldamers.

010405 organic chemistryStereochemistryHydrogen bondChemistry010402 general chemistry01 natural sciences0104 chemical sciencesSurfaces Coatings and FilmsMolecular dynamicsCrystallographyRigidity (electromagnetism)HelixMaterials ChemistryPhysical and Theoretical ChemistryThe journal of physical chemistry. B
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2019

The inner membrane-associated protein of 30 kDa (IM30, also known as Vipp1) is required for thylakoid membrane biogenesis and maintenance in cyanobacteria and chloroplasts. The protein forms large rings of ∼2 MDa and triggers membrane fusion in presence of Mg2+. Based on the here presented observations, IM30 rings are built from dimers of dimers, and formation of these tetrameric building blocks is driven by interactions of the central coiled-coil, formed by helices 2 and 3, and stabilized via additional interactions mainly involving helix 1. Furthermore, helix 1 as well as C-terminal regions of IM30 together negatively regulate ring-ring contacts. We propose that IM30 rings represent the i…

0106 biological sciences0301 basic medicineChemistryLipid bilayer fusionPlant ScienceRing (chemistry)01 natural sciences03 medical and health sciences030104 developmental biologyMembraneThylakoidMembrane biogenesisHelixBiophysicsLipid bilayerBiogenesis010606 plant biology & botanyFrontiers in Plant Science
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Alternative Splicing of the Basic Helix–Loop–Helix Transcription Factor Gene CmbHLH2 Affects Anthocyanin Biosynthesis in Ray Florets of Chrysanthemum…

2021

Chrysanthemum is an important ornamental crop worldwide. Some white-flowered chrysanthemum cultivars produce red ray florets under natural cultivation conditions, but little is known about how this occurs. We compared the expression of anthocyanin biosynthetic and transcription factor genes between white ray florets and those that turned red based on cultivation conditions to comprehend the underlying mechanism. Significant differences in the expression of CmbHLH2 were detected between the florets of different colors. CmbHLH2 generated two alternatively spliced transcripts, designated CmbHLH2Full and CmbHLH2Short. Compared with CmbHLH2Full, CmbHLH2Short encoded a truncated protein with only…

0106 biological sciences0301 basic medicinechrysanthemumMutantPlant Science01 natural sciencesanthocyaninSB1-1110alternative splicing03 medical and health scienceschemistry.chemical_compoundArabidopsisPigment accumulationOriginal Researchbasic helix–loop–helixbiologyChrysanthemum morifoliumAlternative splicingfood and beveragesPlant culturebiology.organism_classificationCell biology030104 developmental biologychemistryMBW complexAnthocyaninRNA splicingHeterologous expression010606 plant biology & botanyFrontiers in Plant Science
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Rigid Core and Flexible Terminus

2012

The structure of the major light-harvesting chlorophyll a/b complex (LHCII) was analyzed by pulsed EPR measurements and compared with the crystal structure. Site-specific spin labeling of the recombinant protein allowed the measurement of distance distributions over several intra- and intermolecular distances in monomeric and trimeric LHCII, yielding information on the protein structure and its local flexibility. A spin label rotamer library based on a molecular dynamics simulation was used to take the local mobility of spin labels into account. The core of LHCII in solution adopts a structure very similar or identical to the one seen in crystallized LHCII trimers with little motional freed…

0106 biological sciences0303 health sciencesPulsed EPRChemistryProtein dynamicsCell BiologySite-directed spin labeling01 natural sciencesBiochemistrylaw.invention03 medical and health sciencesB vitaminsCrystallographyProtein structurelawHelixElectron paramagnetic resonanceSpin labelMolecular Biology030304 developmental biology010606 plant biology & botanyJournal of Biological Chemistry
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The shell matrix of the pulmonate land snail Helix aspersa maxima.

2012

12 pages; International audience; In mollusks, the shell mineralization process is controlled by an array of proteins, glycoproteins and polysaccharides that collectively constitute the shell matrix. In spite of numerous researches, the shell protein content of a limited number of model species has been investigated. This paper presents biochemical data on the common edible land snail Helix aspersa maxima, a model organism for ecotoxicological purposes, which has however been poorly investigated from a biomineralization viewpoint. The shell matrix of this species was extracted and analyzed biochemically for functional in vitro inhibition assay, for amino acid and monosaccharides composition…

0106 biological sciencesBiomineralizationPulmonate snailPhysiology01 natural sciencesBiochemistryMineralization (biology)chemistry.chemical_compoundX-Ray DiffractionTandem Mass SpectrometryElectrophoresis Gel Two-DimensionalHaliotisAmino AcidsComputingMilieux_MISCELLANEOUSchemistry.chemical_classification0303 health sciencesEcologyMonosaccharidesLand snailImmunogold labellingImmunohistochemistryAmino acidBiochemistryElectrophoresis Polyacrylamide GelTerrestrial snail ; biomineralization ; shell ; aragonite ; crossed-lamellar ; protein ; immunogold ; gel electrophoresisFrancefood.ingredientBiology010603 evolutionary biologyCalcium Carbonate03 medical and health sciencesfoodSpecies SpecificityAnimal ShellsShellAnimals14. Life underwater[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular Biology030304 developmental biologyHelix SnailsProteinsCrossed-lamellarbiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsGel electrophoresis[SDV.BA.ZI]Life Sciences [q-bio]/Animal biology/Invertebrate ZoologyCalcium carbonatechemistryMicroscopy Electron ScanningBiomineralizationPinctadaComparative biochemistry and physiology. Part B, Biochemistrymolecular biology
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NMR Investigation of Structures of G-Protein Coupled Receptor Folding Intermediates

2016

Folding of G-protein coupled receptors (GPCRs) according to the two-stage model (Popot, J. L., and Engelman, D. M. (1990) Biochemistry 29, 4031-4037) is postulated to proceed in 2 steps: partitioning of the polypeptide into the membrane followed by diffusion until native contacts are formed. Herein we investigate conformational preferences of fragments of the yeast Ste2p receptor using NMR. Constructs comprising the first, the first two, and the first three transmembrane (TM) segments, as well as a construct comprising TM1-TM2 covalently linked to TM7 were examined. We observed that the isolated TM1 does not form a stable helix nor does it integrate well into the micelle. TM1 is significant…

0301 basic medicine10120 Department of ChemistryBioquímicaSaccharomyces cerevisiae Proteins1303 BiochemistryProtein ConformationStereochemistrySaccharomyces cerevisiaeBiochemistryMicelleRessonància magnètica nuclear1307 Cell BiologyG03 medical and health sciencesprotein coupled receptorGPCRProtein Domains540 Chemistry1312 Molecular BiologyAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyMicellesG protein-coupled receptorSequence Homology Amino Acid030102 biochemistry & molecular biologyChemistryProteïnes de membranaFoldingCell BiologyTransloconPeptide FragmentsTransmembrane proteinNMRFolding (chemistry)Crystallography030104 developmental biologyStructural biology10036 Medical ClinicProtein Structure and FoldingReceptors Mating FactorHelixProtein folding
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Taxonomic clarification of three taxa of Iberian geomitrids, Helix montserratensis Hidalgo, 1870 and subspecies (Gastropoda, Pulmonata), based on mor…

2017

Revisión taxonómica de tres taxones de geomítridos ibéricos, Helix montserratensis Hidalgo, 1870, y subespecies (Gastropoda, Pulmonata), basada en datos morfo–anatómicos Helix montserratensis (actualmente Xerocrassa montserratensis) es un geomítrido ibérico descrito por Hidalgo en 1870 en Montserrat (Barcelona, España). Sobre la base de varios caracteres conquiológicos, se describieron dos taxones muy similares, como variedades de este taxón: Helix montserratensis betulonensis y otro menos nombrado, Helix montserratensis delicatula. Estas variedades, sobre todo betulonensis, se han considerado subespecies de X. montserratensis, aunque algunos autores las consideran especies diferentes, basá…

0301 basic medicineCataloniaSubspeciesMorpho–anatomyPulmonata59 - ZoologiaMol·luscos03 medical and health sciencesType (biology)lcsh:ZoologyGastròpodeslcsh:QL1-991TaxonomyNature and Landscape ConservationMol·luscsbiologyHelix (gastropod)MorphoCatalunyabiology.organism_classification030104 developmental biologyTaxonMolluscaSpainXerocrassa montserratensisDelicatulaAnimal Science and ZoologyXerocrassa montserratensisHumanities
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Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP2

2018

Summary Transient receptor potential (TRP) channels are polymodally regulated ion channels. TRPV4 (vanilloid 4) is sensitized by PIP2 and desensitized by Syndapin3/PACSIN3, which bind to the structurally uncharacterized TRPV4 N terminus. We determined the nuclear magnetic resonance structure of the Syndapin3/PACSIN3 SH3 domain in complex with the TRPV4 N-terminal proline-rich region (PRR), which binds as a class I polyproline II (PPII) helix. This PPII conformation is broken by a conserved proline in a cis conformation. Beyond the PPII, we find that the proximal TRPV4 N terminus is unstructured, a feature conserved across species thus explaining the difficulties in resolving it in previous …

0301 basic medicineChemistryAffinitiesSH3 domainN-terminus03 medical and health sciencesTransient receptor potential channel030104 developmental biologyStructural biologyStructural BiologyHelixBiophysicslipids (amino acids peptides and proteins)Molecular BiologyIon channelPolyproline helixStructure
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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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