Search results for "Protein S"

showing 10 items of 1431 documents

A practical entry to β-aryl-β-alkyl amino alcohols: application to the synthesis of a potent BACE1 inhibitor

2012

The 1,2-addition of alkyl Grignard reagents to readily available N-tert-butanesulfinyl ketimines, bearing an α-silyloxy substituent, proceeds in high yields and excellent diastereocontrol. The utility of the present method was demonstrated by the synthesis, in enantiomerically pure form, of one recently disclosed β-secretase (BACE1) inhibitor.

chemistry.chemical_classificationChemistryArylOrganic ChemistrySubstituentAmino AlcoholsBiochemistrychemistry.chemical_compoundAlzheimer DiseaseReagentPresent methodNitrilesAspartic Acid EndopeptidasesHumansOrganic chemistryIminesAmyloid Precursor Protein SecretasesEnzyme InhibitorsPhysical and Theoretical ChemistryAlkylOrganic & Biomolecular Chemistry
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Synthesis and protonation behaviour of the macrocycle 2,6,10,13,17,21-hexaaza[22]metacyclophane. Thermodynamic and NMR studies on the interaction of …

1996

Abstract The novel cyclophane receptor 2,6,10,13,17,21-hexaaza[22]metacyclophane (L) has been synthesised and characterised. The acid-base behaviour and interaction with ATP, ADP and AMP have been studied by potentiometry in 0.15 mol dm−3 at 298.1 K and multinuclear NMR. L presents in its protonated forms a molecular organization which enables its multipoint binding with nucleotides. Salt-bridge formation occur between the polyammonium sites of L and the phosphate chain of the nucleotides while π-stacking between the meta-phenylene subunit incorporated in the receptor and the adenine ring of the nucleotides.

chemistry.chemical_classificationChemistryStereochemistryProtein subunitProtonationRing (chemistry)Inorganic Chemistrychemistry.chemical_compoundDiamineMaterials ChemistryNucleotideATP–ADP translocasePhysical and Theoretical ChemistryPolyamineCyclophaneInorganica Chimica Acta
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Polypeptide sequence of the chlorophyll a/b/c-binding protein of the prasinophycean alga Mantoniella squamata.

1994

The primary structure of the Chla/b/c-binding protein from Mantoniella squamata is determined. This is the first report that protein sequencing reveals one modified amino acid resulting in a LHCP-specific TFA-cleavage site. The comparison of the sequence of Mantoniella with other Chla/b-and Chla/c-binding proteins shows that the modified amino acid is located in a region which is highly conserved in all these proteins. The alignment also reveals that the LHCP of Mantoniella is related to the Chla/b-binding proteins. Finally, possible Chl-binding regions are discussed.

chemistry.chemical_classificationChlorophyll abiologyBinding proteinProtein primary structureCell BiologyPlant ScienceGeneral Medicinebiology.organism_classificationBiochemistryMolecular biologyAmino acidLight-harvesting complexchemistry.chemical_compoundProtein sequencingBiochemistrychemistryMantoniellaPeptide sequencePhotosynthesis research
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Pigment-pigment interactions and secondary structure of reconstituted algal chlorophyll a/b-binding light-harvesting complexes of Chlorella fusca wit…

1995

Earlier we have shown by in vitro reconstitution experiments that the pigment composition of the chlorophyll alb-binding light-harvesting complex of the green alga Chlorella fusca could be altered in a relatively broad range (Meyer and Wilhelm 1993). In this study we used these reconstituted complexes of different pigment loading to analyze the excitonic interactions between the pigment molecules and the secondary structure by means of circular dichroism spectra in the visible and the far UV spectral regions, respectively. We found that, in contrast to the expectations, the pigment composition and pigment content hardly affected the circular dichroism spectra in the visible spectral region.…

chemistry.chemical_classificationChlorophyll bChlorophyll aCircular dichroismCell BiologyPlant ScienceGeneral MedicineBiologyPhotochemistryBiochemistryLight-harvesting complexchemistry.chemical_compoundPigmentchemistryvisual_artChlorophyllXanthophyllvisual_art.visual_art_mediumsense organsProtein secondary structurePhotosynthesis Research
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Stabilization of an ?-helical conformation in an isolated hexapeptide inhibitor of calmodulin

2001

The conformational properties of two hexapeptides, Ac-LWRILW-NH(2) and its D-amino acid counterpart Ac-lwrilw-NH(2), identified as calmodulin inhibitors using mixture-based synthetic combinatorial library approaches, have been characterised by NMR and CD spectroscopy. The peptides fold into an alpha-helical conformation in aqueous solution. The observed short- and medium-range nuclear Overhauser effects were consistent with the formation of an alpha-helical structure and a reasonably well-defined set of structures was obtained by using restraints from the NMR data in simulated annealing calculations. Analysis of glycine-substitution analogues demonstrated that all the amino acids that make …

chemistry.chemical_classificationCircular dichroismAqueous solutionCalmodulinbiologyStereochemistryOrganic ChemistryBiophysicsGeneral MedicineNuclear magnetic resonance spectroscopyBiochemistryAmino acidPeptide ConformationBiomaterialschemistrybiology.proteinPeptide sequenceProtein secondary structureBiopolymers
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Hierarchical structure formation of cylindrical brush polymer-surfactant complexes.

2009

The complex formation of cylindrical brush polymers with poly(l-lysine) side chains (PLL) and sodium dodecyl sulfate (SDS) can induce a helical conformation of the cylindrical brush polymer in aqueous solution (Gunari, N.; Cong, Y.; Zhang, B.; Fischer, K.; Janshoff, A.; Schmidt, M. Macromol. Rapid Commun. 2008, 29, 821-825). Herein, we have systematically investigated the influence of surfactant, salt, and pH on the supramolecular structure formation. The cylindrical brush polymers and their complexes with surfactants were directly visualized by atomic force microscopy in air and in aqueous solution. The alkyl chain length (measured by the carbon number, n) of the surfactant plays a key rol…

chemistry.chemical_classificationCircular dichroismAqueous solutionMolecular StructureChemistryPolymersSupramolecular chemistrySurfaces and InterfacesPolymerHydrogen-Ion ConcentrationCondensed Matter PhysicsMicroscopy Atomic ForceProtein Structure Secondarychemistry.chemical_compoundSurface-Active AgentsPulmonary surfactantPolymer chemistryElectrochemistrySide chainGeneral Materials ScienceSodium dodecyl sulfateSpectroscopyAlkylLangmuir : the ACS journal of surfaces and colloids
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Conformational investigation of α,β-dehydropeptides VII*. Conformation of Ac-Pro-ΔAla-NHCH3 and Ac-Pro-(E)-ΔAbu-NHCH3: comparison with (Z)-substitute…

2009

The crystal structure and solution conformation of Ac-Pro-deltaAla-NHCH3 and the solution conformation of Ac-Pro-(E)-deltaAbu-NHCH3 were investigated by X-ray diffraction method and NMR, FTIR and CD spectroscopies. Ac-Pro-deltaAla-NHCH3 adopts an extended-coil conformation in the crystalline state, with all-trans peptide bonds and the deltaAla residue being in a C5 form, phi(1)=-71.4(4), psi(1)=-16.8(4), phi(2)= -178.4(3) and psi(2)= 172.4(3) degrees. In inert solvents the peptide also assumes the C5 conformation, but a gamma-turn on the Pro residue cannot be ruled out. In these solvents Ac-Pro-(E)-deltaAbu-NHCH3 accommodates a beta(II)-turn, but a minor conformer with a nearly planar dispo…

chemistry.chemical_classificationCircular dichroismChemistryStereochemistryStereoisomerismPeptideNuclear magnetic resonance spectroscopyBiochemistrychemistry.chemical_compoundCrystallographyProtein structureDehydroalaninePeptide bondConformational isomerismInternational Journal of Peptide and Protein Research
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Inhibition of cyclodextrins on α-galactosidase.

2017

This work successfully investigated the effects of different influential factors and hydrophobic cavities of cyclodextrins (CDs) on α-galactosidase (α-Gal) by detecting α-Gal activity. The highest inhibitory concentration of three kinds of CDs (α-, β-, and γ-CD) on α-Gal was 10mM. Moreover, the highest inhibition of α-Gal was obtained under the following conditions: reaction time of 90min, temperature of 30°C, and pH 6.0. Compared with other CDs, β-CD showed more ability to interact with α-Gal due to its appropriate cavity geometric dimensions. From circular dichroism and nuclear magnetic resonance it was observed that β-CD changed the secondary structure of α-Gal and formed a hydrogen bond…

chemistry.chemical_classificationCircular dichroismCyclodextrinsMagnetic Resonance Spectroscopy010405 organic chemistryChemistryHydrogen bondStereochemistryCircular DichroismTemperatureHydrogen BondingGeneral Medicine010402 general chemistry01 natural sciences0104 chemical sciencesAnalytical ChemistryCrystallographyα galactosidaseEnzymealpha-GalactosidaseProtein secondary structureFood ScienceFood chemistry
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Revisiting Secondary Structures in NCA Polymerization: Influences on the Analysis of Protected Polylysines

2014

Two series (degree of polymerization: 20–200) of polylysines with Z and TFA protecting groups were synthesized, and their behavior in a range of analytical methods was investigated. Gel permeation chromatography of the smaller polypeptides reveals a bimodal distribution, which is lost in larger polymers. With the help of GPC, NMR, circular dichroism (CD), and MALDI-TOF, it was demonstrated that the bimodal distribution is not due to terminated chains or other side reactions. Our results indicate that the bimodality is caused by a change in secondary structure of the growing peptide chain that occurs around a degree of polymerization of about 15. This change in secondary structure interferes…

chemistry.chemical_classificationCircular dichroismPolymers and PlasticsOrganic ChemistryPeptidePolymerDegree of polymerizationRandom coilInorganic ChemistryGel permeation chromatographychemistryPolymerizationPolymer chemistryMaterials ChemistryProtein secondary structureMacromolecules
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Influence of the hydrophilic face on the folding ability and stability of α-helix bundles: relevance to the peptide catalytic activity

2000

Although not the sole feature responsible, the packing of amino acid side chains in the interior of proteins is known to contribute to protein conformational specificity. While a number of amphipathic peptide sequences with optimized hydrophobic domains has been designed to fold into a desired aggregation state, the contribution of the amino acids located on the hydrophilic side of such peptides to the final packing has not been investigated thoroughly. A set of self-aggregating 18-mer peptides designed previously to adopt a high level of alpha-helical conformation in benign buffer is used here to evaluate the effect of the nature of the amino acids located on the hydrophilic face on the pa…

chemistry.chemical_classificationCrystallographyEndocrinologyProtein structurechemistryProtein designProtein foldingPeptideBiochemistryPeptide sequenceProtein tertiary structureAlpha helixAmino acidThe Journal of Peptide Research
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