Search results for "PEPTIDE"

showing 10 items of 4589 documents

ChemInform Abstract: Modified Trityl Ester Protecting Groups in Peptide Synthesis.

2010

chemistry.chemical_compoundchemistryPeptide synthesisOrganic chemistryGeneral MedicineCombinatorial chemistryChemInform
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1982

chemistry.chemical_compoundchemistryPolymer sciencePolymer chemistryPeptide synthesisDie Makromolekulare Chemie, Rapid Communications
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Surfactant-assisted chromogenic sensing of cyanide in water

2009

Chromogenic cyanide recognition in water was achieved by the use of a hydrophobic dye in micellar containers.

chemistry.chemical_compoundchemistryPulmonary surfactantChromogenicCyanideInorganic chemistrytechnology industry and agricultureMaterials ChemistryOrganic chemistrylipids (amino acids peptides and proteins)macromolecular substancesGeneral ChemistryCatalysisNew Journal of Chemistry
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Longitudinal associations of physical activity and sedentary time with cardiometabolic risk factors in children

2019

Background: There are few prospective studies on the associations of changes in objectively measured vigorous physical activity (VPA∆), moderate‐to‐vigorous physical activity (MVPA∆), light physical activity (LPA∆), and sedentary time (ST∆) with changes in cardiometabolic risk factors (∆) in children. We therefore investigated these relationships among children. Methods: The participants were a population sample of 258 children aged 6‐8 years followed for 2 years. We assessed PA and ST by a combined heart rate and movement sensor; computed continuous age‐ and sex‐adjusted z‐scores for waist circumference, blood pressure, and fasting insulin, glucose, triglycerides, and high‐density lipoprot…

childrenterveydentilaphysical activitylipids (amino acids peptides and proteins)riskitekijätpitkittäistutkimusliikuntacardiometabolic risk factorslapsetfyysinen aktiivisuus
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S-type lectins occur also in invertebrates: high conservation of the carbohydrate recognition domain in the lectin genes from the marine sponge Geodi…

1993

The marine sponge Geodia cydonium contains several lectins. The main component, called lectin-1, is composed of three to four identical subunits. The subunits of the lectins were cloned from a cDNA library; two clones were obtained. From the deduced aa sequence of one clone, LECT-1, a mol. wt of 15,313 Da is calculated; this value is in good agreement with mass spectrometric analysis of 15,453 +/- 25 Da. The sequence of another clone, LECT-2, was analysed and the aa sequence was deduced (15,433 Da). The two subunits have a framework sequence of 38 conserved aa which are characteristic for the carbohydrate-binding site of vertebrate S-type lectins. Clustering of lectin sequences of various s…

clone (Java method)GalectinsBlotting WesternMolecular Sequence DataBiochemistryChromatography AffinityMass SpectrometryLectinsAnimalsAmino Acid SequenceCloning MolecularPeptide sequenceGeneGalectinCloningbiologyBase SequencecDNA libraryLectinDNAbiology.organism_classificationPoriferaSuberites domunculaBiochemistrybiology.proteinElectrophoresis Polyacrylamide GelGlycobiology
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Associations of dietary carbohydrate and fatty acid intakes with cognition among children

2020

Objective: To investigate the cross-sectional associations of dietary carbohydrate and fatty acid intakes with cognition in mid-childhood. Design: Dietary carbohydrate and fatty acid intakes were assessed using 4-d food records, and cognition was evaluated using the Raven’s Coloured Progressive Matrices (RCPM) score. The cross-sectional associations of dietary carbohydrate and fatty acid intakes with cognition were investigated using linear regression analyses adjusted for age, sex, body fat percentage, household income, parental education and daily energy intake. Setting: The baseline examinations of the Physical Activity and Nutrition in Children study. Participants: A population-based sa…

cognitionkognitiochildrencarbohydratebrainrasvahapotlipids (amino acids peptides and proteins)lapset (ikäryhmät)fatty aciddietruokavaliotaivothiilihydraatit
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Conformational investigation of α,β‐dehydropeptides. XV: N‐acetyl‐α,β‐dehydroamino acid N ′N ′‐dimethylamides: conformational properties from infrare…

2005

The FTIR spectra were analysed in the region of the nu(s)(N-H), AI(C=O) and nu(s)(Calpha=Cbeta) bands for a series of Ac-DeltaXaa-NMe2, where DeltaXaa = DeltaAla, (Z)-DeltaAbu, (Z)-DeltaLeu, (Z)-DeltaPhe and DeltaVal, to determine a predominant solution conformation of these alpha,beta-dehydropeptide-related molecules. Measurements were taken in CCl4, DCM and MeCN solutions. In the same way, spectra of saturated analogues Ac-Xaa-NMe2, where Xaa = Ala, Abu, Leu, Phe and Val, were investigated. To help interpret the spectroscopic results, conformational maps were calculated by the B3LYP/6-31+G** method. Also, the relative energies of all conformers of the dehydro compounds in vacuo as well as…

conformationStereochemistryProtein ConformationαPeptideamide/π(Ph) interactionBiochemistrySpectral linechemistry.chemical_compoundStructural BiologyAmideDrug DiscoverySpectroscopy Fourier Transform InfraredSide chainMoleculeC5 hydrogen bondFourier transform infrared spectroscopysolute/solvent interactionMolecular BiologyConformational isomerismβ‐dehydroamino acidsPharmacologychemistry.chemical_classificationChemistryHydrogen bondOrganic ChemistryGeneral MedicineModels TheoreticalAmidestheoretical IR frequenciesFTIR spectroscopyMolecular Medicinedensity functional theory calculationsPeptidesJournal of Peptide Science
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Partial thioamide scan on the lipopeptaibiotic trichogin GA IV. Effects on folding and bioactivity

2012

Backbone modification is a common chemical tool to control the conformation of linear peptides and to explore potentially useful effects on their biochemical and biophysical properties. The thioamide, ψ[CS-NH], group is a nearly isosteric structural mimic of the amide (peptide) functionality. In this paper, we describe the solution synthesis, chemical characterization, preferred conformation, and membrane and biological activities of three, carefully selected, peptide analogues of the lipopeptaibiotic [Leu11-OMe] trichogin GA IV. In each analogue, a single thioamide replacement was incorporated. Sequence positions near the N-terminus, at the center, and near the C-terminus were investigated…

conformationbioactivity; conformation; peptaibiotic; peptide synthesis; peptides; thiopeptidesSequence (biology)PeptideFull Research Paperlcsh:QD241-441peptaibioticchemistry.chemical_compoundlcsh:Organic chemistryAmidepeptide synthesisPeptide synthesislcsh:ScienceThioamidechemistry.chemical_classificationconformation; peptaibiotic; peptide synthesis; thiopeptides; bioactivityOrganic ChemistryLipopeptideCombinatorial chemistryFolding (chemistry)ChemistryMembranechemistrythiopeptidesbioactivitypeptideslcsh:QBeilstein Journal of Organic Chemistry
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Crystal structure of the tripeptideN-(benzyloxycarbonyl)glycylglycyl-L-norvaline

2015

The title tripeptide, C17H23N3O6, contains a nonproteinogenic C-terminal amino acid residue, norvaline, which is an isomer of the amino acid valine. Norvaline, unlike valine, has an unbranched side chain. The molecule has a Gly–Gly segment which adopts an extended conformation. The norvaline residue also adopts an extended backbone conformation while its side chain has ag+tconformation. In the crystal lattice, N—H...O and O—H...O hydrogen bonds stabilize the packing. Molecules translated along the crystallographicaaxis associate through an N—H...O hydrogen bond. The remaining three hydrogen bonds are between molecules related by a21screw axis.

conformationchemistry.chemical_classificationcrystal structureStereochemistryHydrogen bondGeneral ChemistryTripeptideCrystal structurehydrogen bondingCondensed Matter PhysicsData ReportspeptidenorvalineAmino acidlcsh:Chemistrychemistry.chemical_compoundResidue (chemistry)lcsh:QD1-999chemistryValineSide chainGeneral Materials ScienceNorvalineglycineActa Crystallographica Section E Crystallographic Communications
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Conformational investigation of α,β‐dehydropeptides Part VI. Molecular and crystal structure of benzyloxycarbonylglycyl‐(Z )‐dehydrophenylalanine

1994

The structure of a peptide containing C-terminal dehydrophenylalanine, Z-Gly-(Z)-delta Phe (C19H18N2O5, MW = 354) was determined from single-crystal X-ray diffraction data. Needle-shaped crystals were grown from a 1:1 mixture of methanol-acetone in the monoclinic space group P2(1) with a = 14.717(4), b = 4.941(2), c = 12.073(4) A, beta = 103.72(4) degrees; V = 852.86(8) A3, Z = 2 and Dc = 1.32 g cm-3. The structure was solved by direct methods using SHELXS-86 and refined to a final R-index of 0.032 for 1714 observed reflections. The peptide adopts a conformation folded at the glycine residue, and principal torsion angles are omega 0 = -167.6(2) degrees, phi 1 = -71.8(3) degrees, psi 1 = -31…

conformationdehydropeptidehydrogen bondProtein ConformationChemistryHydrogen bondhelical conformersIntermolecular forceDipeptidesCrystal structuredehydrophenylalanineBiochemistryZ‐Gly‐(Z )‐APheCrystallographyProtein structureX-Ray DiffractionIntramolecular forceSpectroscopy Fourier Transform InfraredX-ray crystallographyMoleculeinfrared spectroscopyX‐ray structure analysisMonoclinic crystal systemInternational Journal of Peptide and Protein Research
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