Search results for "protein conformation"

showing 10 items of 515 documents

Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches

2013

The tyrosinase gene from Ralstonia solanacearum (GenBank NP518458) was subjected to random mutagenesis resulting in tyrosinase variants (RVC10 and RV145) with up to 3.2-fold improvement in kcat, 5.2-fold lower Km and 16-fold improvement in catalytic efficiency for D-tyrosine. Based on RVC10 and RV145 mutated sequences, single mutation variants were generated with all variants showing increased kcat for D-tyrosine compared to the wild type (WT). All single mutation variants based on RV145 had a higher kcat and Km value compared to the RV145 and thus the combination of four mutations in RV145 was antagonistic for turnover, but synergistic for affinity of the enzyme for D-tyrosine. Single muta…

DNA BacterialProtein ConformationSequence analysisTyrosinasehomology modelingMolecular Sequence DataMutation Missenserandom mutagenesisBioengineeringtyrosinaseProtein Engineering010402 general chemistry01 natural sciencesApplied Microbiology and Biotechnologyenzyme catalysis03 medical and health sciencessite specific mutagenesisMissense mutationSite-directed mutagenesisHistidine030304 developmental biology0303 health sciencesRalstonia solanacearumbiologyMonophenol MonooxygenaseWild typeActive siteSequence Analysis DNAbiology.organism_classificationMolecular biologyRecombinant Proteins0104 chemical sciencesKineticsMutagenesisRalstonia solanacearumbiology.proteinTyrosineD-tyrosineMutant ProteinsBiotechnology
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Molecular characterization of a phosphoenolpyruvate carboxylase in the gymnosperm Picea abies (Norway spruce)

1996

Phosphoenolpyruvate carboxylase (PEPC) genes and cDNA sequences have so far been isolated from a broad range of angiosperm but not from gymnosperm species. We constructed a cDNA library from seedlings of Norway spruce (Picea abies) and identified cDNAs coding for PEPC. A full-length PEPC cDNA was sequenced. It consists of 3522 nucleotides and has an open reading frame (ORF) that encodes a polypeptide (963 amino acids) with a molecular mass of 109551. The deduced amino acid sequence revealed a higher similarity to the C3-form PEPC of angiosperm species (86-88%) than to the CAM and C4 forms (76-84%). The putative motif (Lys/Arg-X-X-Ser) for serine kinase, which is conserved in all angiosperm …

DNA ComplementaryDNA PlantProtein ConformationMolecular Sequence DataPlant ScienceBiologyTreesEvolution MolecularGymnospermComplementary DNABotanyGeneticsAmino Acid SequenceRNA MessengerCloning MolecularPeptide sequencePhylogenySouthern blotBase SequenceSequence Homology Amino AcidcDNA libraryHybridization probefungifood and beveragesPicea abiesGeneral MedicineBlotting Northernbiology.organism_classificationPhosphoenolpyruvate CarboxylaseBlotting SouthernBiochemistryPhosphoenolpyruvate carboxylaseAgronomy and Crop SciencePlant Molecular Biology
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Interfacial water structure controls protein conformation.

2007

A phenomenological theory of salt-induced Hofmeister phenomena is presented, based on a relation between protein solubility in salt solutions and protein-water interfacial tension. As a generalization of previous treatments, it implies that both kosmotropic salting out and chaotropic salting in are manifested via salt-induced changes of the hydrophobic/hydrophilic properties of protein-water interfaces. The theory is applied to describe the salt-dependent free energy profiles of proteins as a function of their water-exposed surface area. On this basis, three classes of protein conformations have been distinguished, and their existence experimentally demonstrated using the examples of bacter…

DYNAMICSMECHANISMKosmotropicProtein ConformationSURFACE-TENSIONSurface tensionchemistry.chemical_compoundProtein structureMaterials ChemistryPhysical and Theoretical ChemistryPURPLE MEMBRANESPECTROSCOPYbiologySTABILITYBACTERIORHODOPSINMyoglobinSALTTemperatureWaterBacteriorhodopsinSTABILITY MECHANISMSurfaces Coatings and FilmsION SPECIFICITYChaotropic agentCrystallographyMyoglobinchemistryTEMPERATURE-DEPENDENCEChemical physicsStructural stabilityBacteriorhodopsinsbiology.proteinSalting outThermodynamicsThe journal of physical chemistry. B
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Principal component analysis on molecular descriptors as an alternative point of view in the search of new Hsp90 inhibitors

2009

Inhibiting a protein that regulates multiple signal transduction pathways in cancer cells is an attractive goal for cancer therapy. Heat shock protein 90 (Hsp90) is one of the most promising molecular targets for such an approach. In fact, Hsp90 is a ubiquitous molecular chaperone protein that is involved in folding, activating and assembling of many key mediators of signal transduction, cellular growth, differentiation, stress-response and apoptothic pathways. With the aim to analyze which molecular descriptors have the higher importance in the binding interactions of these classes, we first performed molecular docking experiments on the 187 Hsp90 inhibitors included in the BindingDB, a pu…

Databases FactualProtein ConformationDrug Evaluation PreclinicalCancer therapyPrincipal component analysiNaphtholsBiochemistryBinding databaseMolecular descriptorsStructure-Activity RelationshipStructural BiologyMolecular descriptorHeat shock proteinComputer SimulationHSP90 Heat-Shock ProteinsPrincipal Component AnalysisBinding SitesbiologyHeat shock proteinOrganic ChemistryComputational BiologyIsoxazolesHsp90Settore CHIM/08 - Chimica FarmaceuticaComputational MathematicsBiochemistryPurinesDocking (molecular)Principal component analysisMolecular dockingbiology.proteinPyrazolesBindingDBSignal transduction
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Enhanced β-turn conformational stability of tripeptides containing Δphe in cis over trans configuration

2013

Conformations of three pairs of dehydropeptides with the opposite configuration of the Delta Phe residue, Boc-Gly-Delta(Z/E)Phe-Phe-p-NA (Z- p -NA and E- p -NA), Boc-Gly-Delta(Z/E)Phe-Phe-OMe (Z-OMe and E-OMe), and Boc-Gly-Delta(Z/E)Phe-Phe-OH (Z-OH and E-OH) were compared on the basis of CD and NMR studies in MeOH, TFE, and DMSO. The CD results were used as the additional input data for the NMR-based calculations of the detailed solution conformations of the peptides. It was found that Z- p -NA, E- p -NA, Z-OMe, and Z-OH adopt the beta-turn conformations and E-OMe and E-OH are unordered. There are two overlapping type III beta-turns in Z- p -NA, type II' beta-turn in E- p -NA, and type II …

Dehydropeptide conformationCircular dichroismMagnetic Resonance SpectroscopyStereochemistryProtein ConformationPhenylalanineClinical BiochemistryTripeptideCircular dichroismTemperature coefficients of amide protonsBiochemistryNuclear magnetic resonancechemistry.chemical_compoundResidue (chemistry)Trans configurationchemistry [Oligopeptides]Amideotorhinolaryngologic diseasesHydrogen bondProtein StabilityDehydropeptidesCircular DichroismOrganic ChemistryStereoisomerismchemistryIntramolecular forceddc:540Dehydrophenylalanine configurationchemical synthesis [Oligopeptides]Conformational stabilitychemistry [Phenylalanine]OligopeptidesAmino Acids
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Biofabrication of biosilica-glass by living organisms

2008

Biosilicification is an evolutionarily old and widespread type of biomineralization both in unicellular and multicellular organisms, including sponges, diatoms, radiolarians, choanoflagellates, and higher plants. In the last few years combined efforts in molecular biology, cell biology, and inorganic and analytical chemistry have allowed the first insight into the molecular mechanisms by which these organisms form an astonishing variety of siliceous structures that cannot be achieved by chemical methods. Here we report about the present stage of knowledge on structure, biochemical composition, and mechanisms of biosilica formation, focusing our attention particularly on sponges because of t…

DiatomsModels MolecularSequence Homology Amino AcidProtein ConformationMolecular Sequence DataOrganic ChemistryBiologySilicon DioxideCathepsinsBiochemistryPoriferaMulticellular organismSequence homologyEvolutionary biologyDrug DiscoveryBiochemical compositionAnimalsGlassBiomineralizationBiofabricationNatural Product Reports
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How is the inner circadian clock controlled by interactive clock proteins?

2015

AbstractMost internationally travelled researchers will have encountered jetlag. If not, working odd hours makes most of us feel somehow dysfunctional. How can all this be linked to circadian rhythms and circadian clocks? In this review, we define circadian clocks, their composition and underlying molecular mechanisms. We describe and discuss recent crystal structures of Drosophila and mammalian core clock components and the enormous impact they had on the understanding of circadian clock mechanisms. Finally, we highlight the importance of circadian clocks for the daily regulation of human/mammalian physiology and show connections to overall fitness, health and disease.

Drosophila and mammalian clock proteinCircadian rhythmCircadian clock mechanismProtein ConformationCircadian clockBiophysicsCLOCK Proteins3D crystal structureCell BiologyBiologyBiochemistryBacterial circadian rhythmsCell biologyStructural BiologyCircadian ClocksGeneticsAnimalsHumansCLOCK ProteinsCircadian rhythmOscillating geneMolecular BiologyNeuroscienceFEBS Letters
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X-ray crystallography-promoted drug design of carbonic anhydrase inhibitors.

2015

1-N-Alkylated-6-sulfamoyl saccharin derivatives were prepared and assayed as carbonic anhydrase inhibitors (CAIs). During X-ray crystallographic experiments an unexpected hydrolysis of the isothiazole ring was evidenced which allowed us to prepare highly potent enzyme inhibitors with selectivity for some isoforms with medical applications.

DrugModels MolecularStereochemistryProtein Conformationmedia_common.quotation_subjectCrystallography X-RayCatalysisHydrolysischemistry.chemical_compoundCarbonic anhydraseMaterials ChemistryHumansCarbonic Anhydrase Inhibitorsmedia_commonCarbonic Anhydraseschemistry.chemical_classificationIsothiazolebiologyMetals and AlloysGeneral ChemistryLyaseSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsIsoenzymesEnzymechemistryDrug DesignX-ray crystallographyCeramics and Compositesbiology.proteinSelectivityChemical communications (Cambridge, England)
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Toward a Rationale for the PTC124 (Ataluren) Promoted Readthrough of Premature Stop Codons: A Computational Approach and GFP-Reporter Cell-Based Assay

2014

The presence in the mRNA of premature stop codons (PTCs) results in protein truncation responsible for several inherited (genetic) diseases. A well-known example of these diseases is cystic fibrosis (CF), where approximately 10% (worldwide) of patients have nonsense mutations in the CF transmembrane regulator (CFTR) gene. PTC124 (3-(5-(2-fluorophenyl)-1,2,4-oxadiazol-3-yl)-benzoic acid), also known as Ataluren, is a small molecule that has been suggested to allow PTC readthrough even though its target has yet to be identified. In the lack of a general consensus about its mechanism of action, we experimentally tested the ability of PTC124 to promote the readthrough of premature termination c…

Duchenne muscular distrophy (DMD)Protein ConformationNonsense mutationBlotting WesternGreen Fluorescent ProteinsPharmaceutical ScienceCystic Fibrosis Transmembrane Conductance RegulatorSettore BIO/11 - Biologia MolecolareBiologyMolecular Dynamics Simulationmedicine.disease_causeReal-Time Polymerase Chain Reactionpremature termination codons (PTC)ArticleGreen fluorescent proteinchemistry.chemical_compoundDrug DiscoverymedicineCoding regionHumansRNA Messengermolecular dynamics (MD)GeneCells CulturedGeneticsnonsense mutation readthroughMessenger RNAMutationOxadiazolesReverse Transcriptase Polymerase Chain Reactiongreen fluorescent protein (GFP)atalurenSettore CHIM/06 - Chimica OrganicaStop codonAtalurenSettore BIO/18 - GeneticachemistryCodon NonsenseSettore CHIM/03 - Chimica Generale E InorganicaMutationCodon TerminatorMutagenesis Site-DirectedMolecular MedicineNucleic Acid Conformationcystic fibrosis (CF)oxadiazoleHeLa Cells
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The hydration shell of myoglobin.

1992

The space in the unit cell of a metmyoglobin crystal not occupied by myoglobin atoms was filled with water using Monte Carlo calculations. Independent calculations with different amounts of water have been performed. Structure factors were calculated using the water coordinates thus obtained and the known coordinates of the myoglobin atoms. A comparison with experimental structure factors showed that both the low and the high resolution regime could be well reproduced with 814 Monte Carlo water molecules per unit cell with a B-value of 50 A2. The Monte Carlo water molecules yield a smaller standard R-value (0.166) than using a homogeneous electron density for the simulation of the crystal w…

Electron densityMyoglobinProtein ConformationMonte Carlo methodBiophysicsWaterGeneral MedicineCrystal structureMolecular physicsCrystalCrystallographyReciprocal latticechemistry.chemical_compoundSolvation shellMyoglobinchemistryX-Ray DiffractionYield (chemistry)Monte Carlo MethodProtein BindingEuropean biophysics journal : EBJ
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