Search results for "Valine"

showing 10 items of 85 documents

Chromatographic and mass spectrometric characterization of the structures of the polypeptide antibiotics samarosporin and stilbellin and identity wit…

1983

The structural identity of the polypeptide antibiotics, samarosporin I(II) and stilbellin I(II) with emerimicin IV(III) has been established by thin-layer chromatography, quantitative amino acid analysis by ion-exchange chromatography, gas-liquid chromatography of the N-pentafluoropropionyl amino acid n-propyl esters and N,O-bis-pentafluoropropionyl phenylalaninol with quartz capillaries coated with the chiral stationary phase N-propionyl-L-valine-tert-butylamide, and determination of the relative molecular masses and sequence-specific fragments by field desorption fast atom bombardment mass spectrometry. The separation of closely related sequence analogues of the above polypeptides could b…

chemistry.chemical_classificationAqueous solutionChromatographyChemistryOrganic ChemistryClinical BiochemistryPeptaibolFast atom bombardmentMass spectrometryBiochemistryAnalytical ChemistryAmino acidchemistry.chemical_compoundColumn chromatographyIsovalineMoleculeOrganic chemistryChromatographia
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l-Valine biosynthesis during batch and fed-batch cultivations of Corynebacterium glutamicum: Relationship between changes in bacterial growth rate an…

2007

Abstract A transition in the bacterial growth rate to below maximum was found to be an optimum parameter of cellular physiology to increase the activity of acetohydroxy acid synthase, a regulatory enzyme in l -valine synthesis, and amino acid overproduction by Corynebacterium glutamicum ATCC 13032 recombinants under batch and fed-batch cultivation conditions. An increase in l -valine synthesis under transient situations when cellular growth rate was downregulated was correlated to a decrease in the activity of aconitase, a key enzyme in the tricarboxylic acid cycle (TCA) of C. glutamicum , and, in contrast, to an increase in the activity of glucose-6-phosphate dehydrogenase, a key enzyme in…

chemistry.chemical_classificationBioengineeringMetabolismPentose phosphate pathwayBiologyApplied Microbiology and BiotechnologyBiochemistryAconitaseAmino acidCorynebacterium glutamicumCitric acid cyclechemistryBiochemistryValineAmino acid synthesisProcess Biochemistry
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A Co2O2 metallacycle exclusively supported by l-valine

2008

Abstract [Co2(OH)2( l -valine)4]·2.5H2O has been prepared under hydrothermal conditions and constitutes the first example of a [Co2O2] core supported exclusively by aminoacids. This synthetic dimetallic model for redox active metalloenzymes is one of the few binary aminoacid compounds of biologically relevant metal ions that has been structurally characterized, showing the possibilities of this synthetic approach for preparation of models in bioinorganic chemistry.

chemistry.chemical_classificationChemistryStereochemistryMetal ions in aqueous solutionBioinorganic chemistryGeneral ChemistryMetallacycleCondensed Matter PhysicsAmino acidValineHydrothermal synthesisGeneral Materials ScienceChirality (chemistry)Group 2 organometallic chemistrySolid State Sciences
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Synthese sterisch gehinderter Peptide und Depsipeptide nach einem Säurechlorid-Verfahren mit 2-Phosphonioethoxycarbonyl-(Peoc-)Aminosäuren und -Hydro…

1982

2-(Triphenylphosphonio)ethoxycarbonyl-(Peoc-)aminosauren 1 und -hydroxysauren 5 werden mit Oxalylchlorid in bei Raumtemp. stabile Saurechloride 2 bzw. 6 ubergefuhrt. Mit diesen aktivierten Verbindungen werden sterisch gehinderte Amidbindungen — z. B. in den geschutzten Valin-Peptiden 3a—g und in Hydroxyacyl-Dipeptiden 7 — hergestellt. Nach Schutzgruppenabspaltung aus der voll geschutzten Form 7a entsteht so die Sporidesmolsaure B (9a), die in ihren Eigenschaften mit dem Abbauprodukt aus dem Sporidesmolid I ubereinstimmt. Trotz zweimaliger Anwendung der Saurechlorid-Kondensation ist keine Racemisierung eingetreten. Syntheses of Sterically Hindered Peptides and Depsipeptides by Means of an Ac…

chemistry.chemical_classificationDepsipeptideSteric effectsStereochemistryOrganic ChemistryChlorideAmino acidchemistry.chemical_compoundOxalyl chloridechemistryValinemedicinePhysical and Theoretical ChemistryAmide bondsmedicine.drugLiebigs Annalen der Chemie
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Risk Assessment of "Other Substances" – L-leucine, L-isoleucine and L-valine, the Branched Chain Amino Acids (BCAA)

2018

chemistry.chemical_classificationFood supplementchemistryBiochemistryValineAdverse health effectL-IsoleucineLeucineAmino acidEuropean Journal of Nutrition & Food Safety
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Untersuchungen zur Aminos�ureimbalanz

1957

chemistry.chemical_classificationLitter (animal)MethionineChemistryLysineTryptophanGeneral MedicineAmino acidchemistry.chemical_compoundmedicine.anatomical_structureBiochemistryValineLactationDrug DiscoverymedicineMolecular MedicineLeucineGenetics (clinical)Klinische Wochenschrift
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Molecular aggregation in selected crystalline 1:1 complexes of hydrophobicD- andL-amino acids. IV. TheL-phenylalanine series

2009

The amino acid L-phenylalanine has been cocrystallized with D-2-aminobutyric acid, C(9)H(11)NO(2).C(4)H(9)NO(2), D-norvaline, C(9)H(11)NO(2).C(5)H(11)NO(2), and D-methionine, C(9)H(11)NO(2).C(5)H(11)NO(2)S, with linear side chains, as well as with D-leucine, C(9)H(11)NO(2).C(6)H(13)NO(2), D-isoleucine, C(9)H(11)NO(2).C(6)H(13)NO(2), and D-allo-isoleucine, C(9)H(11)NO(2).C(6)H(13)NO(2), with branched side chains. The structures of these 1:1 complexes fall into two classes based on the observed hydrogen-bonding pattern. From a comparison with other L:D complexes involving hydrophobic amino acids and regular racemates, it is shown that the structure-directing properties of phenylalanine closel…

chemistry.chemical_classificationMolecular StructureChemistryStereochemistryAminobutyratesPhenylalanineHydrogen BondingStereoisomerismStereoisomerismPhenylalanineGeneral MedicineCrystallography X-RayGeneral Biochemistry Genetics and Molecular BiologyAmino acidValineSide chainIsoleucineLeucineAminobutyratesHydrophobic and Hydrophilic InteractionsActa Crystallographica Section C Crystal Structure Communications
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Enantioselective self-assembly of antiferromagnetic hexacopper(ii) wheels with chiral amino acid oxamates

2013

The Cu(2+)-mediated self-assembly of oxamato-based ligands derived from either the (S)- or (R)-enantiomers of the amino acid valine leads to the formation of two antiferromagnetically coupled homochiral anionic hexacopper(II) wheels in the presence of templating tetramethylammonium countercations.

chemistry.chemical_classificationTetramethylammoniumStereochemistryMagnetic PhenomenaMetals and AlloysEnantioselective synthesisStereoisomerismValineGeneral ChemistryLigandsCatalysisSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsAmino acidchemistry.chemical_compoundchemistryCoordination ComplexesValineMaterials ChemistryCeramics and CompositesAntiferromagnetismSelf-assemblyCopperChemical Communications
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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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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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