0000000000605741

AUTHOR

Jesús Jiménez-barbero

0000-0001-5421-8513

showing 4 related works from this author

Mechanism of sulfur transfer across protein-protein interfaces: The cysteine desulfurase model system

2016

CsdA cysteine desulfurase (the sulfur donor) and the CsdE sulfur acceptor are involved in biological sulfur trafficking and in iron-sulfur cluster assembly in the model bacterium Escherichia coli. CsdA and CsdE form a stable complex through a polar interface that includes CsdA Cys328 and CsdE Cys61, the two residues known to be involved in the sulfur transfer reaction. Although mechanisms for the transfer of a sulfur moiety across protein-protein interfaces have been proposed based on the IscS-IscU and IscS-TusA structures, the flexibility of the catalytic cysteine loops involved has precluded a high resolution view of the active-site geometry and chemical environment for sulfur transfer. H…

inorganic chemicals0301 basic medicineChemistryCysteine desulfuraseInorganic chemistrychemistry.chemical_elementIsothermal titration calorimetryGeneral Chemistry010402 general chemistry01 natural sciencesCombinatorial chemistryAcceptorSulfurCatalysis0104 chemical sciences03 medical and health sciences030104 developmental biologyMoietyTransferaseBiogenesisCysteine
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New Cathepsin Inhibitors to Explore the Fluorophilic Properties of the S 2 Pocket of Cathepsin B: Design, Synthesis, and Biological Evaluation

2011

5 páginas, 1 figura, 2 tablas -- PAGS nros. 5256-5260

Hydrocarbons FluorinatedStereochemistryStereoisomerismhydrolasesstereoselectivityCatalysisCathepsin BCathepsin BNitrilesinhibitorsCombinatorial Chemistry TechniquesHumansMoleculefluorinated ligandsBiological evaluationCathepsinMolecular StructureCombinatorial Chemistry TechniquesligandsChemistryOrganic ChemistryStereoisomerismDipeptidesGeneral Chemistryfluorinated fluorinatedDesign synthesisDrug DesignpeptidesStereoselectivityChemistry – A European Journal
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On the Importance of Carbohydrate-Aromatic Interactions for the Molecular Recognition of Oligosaccharides by Proteins: NMR Studies of the Structure a…

2005

The specific interaction of a variety of modified hevein domains to chitooligosaccharides has been studied by NMR spectroscopy in order to assess the importance of aromatic-carbohydrate interactions for the molecular recognition of neutral sugars. These mutant AcAMP2-like peptides, which have 4-fluoro-phenylalanine, tryptophan, or 2-naphthylalanine at the key interacting positions, have been prepared by solid-phase synthesis. Their three-dimensional structures, when bound to the chitin-derived trisaccharide, have been deduced by NMR spectroscopy. By using DYANA and restrained molecular dynamics simulations with the AMBER 5.0 force field, the three-dimensional structures of the protein-sugar…

chemistry.chemical_classificationStereochemistryMolecular Sequence DataOrganic ChemistryEnthalpyTryptophanOligosaccharidesProteinsAromaticityGeneral ChemistryNuclear magnetic resonance spectroscopyCatalysisMolecular dynamicsMolecular recognitionchemistryThermodynamicsAmino Acid SequenceTrisaccharidePeptidesNuclear Magnetic Resonance BiomolecularPeptide sequenceChemistry - A European Journal
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Antimicrobial Peptides and Their Superior Fluorinated Analogues: Structure-Activity Relationships as Revealed by NMR Spectroscopy and MD Calculations

2010

9 pag., 6 fig, 3 tab.

Models MolecularMagnetic Resonance SpectroscopyHalogenationProtein ConformationDiffusionAntimicrobial peptidesMicrobial Sensitivity TestsMolecular Dynamics SimulationBiochemistryMicelleStructure-Activity RelationshipMolecular dynamicsantimicrobial peptidesNMR spectroscopyComputational chemistryfluorineEscherichia coliOrganic chemistryAmino Acid SequenceMolecular BiologyAqueous solutionMolecular StructureChemistryOrganic ChemistrySodium Dodecyl SulfateWaterNuclear magnetic resonance spectroscopyAntimicrobialmolecular dynamicsSolutionsMembranemembranespeptidesMolecular MedicineAntimicrobialSDS micellesOligopeptidesAntimicrobial Cationic Peptides
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