Search results for "conformation"

showing 10 items of 1414 documents

Characterisation of rpsL, rrs and embB mutations associated with streptomycin and ethambutol resistance in Mycobacterium tuberculosis.

2003

In order to characterise molecular mechanisms of first-line drug resistance in Mycobacterium tuberculosis and to evaluate the use of molecular markers of resistance (gene point mutations), we analysed 66 multi-drug-resistant (MDR) isolates from Latvian tuberculosis patients. They were all resistant to rifampin (RIF), isoniazid (INH) and streptomycin (SM), and 33 were resistant to ethambutol (EMB). Enzymatic digestion by MboII and nucleotide sequencing of the rpsL gene fragment detected a single nucleotide substitution K43R in 40 (61%) of the 66 SM-resistant M. tuberculosis isolates. Of the other 26 SM-resistant isolates, 16 (24%) had mutations at positions 513A--C and 516C--T of the rrs gen…

DNA BacterialRibosomal ProteinsDrug resistanceGene mutationMicrobiologyPolymerase Chain ReactionMycobacterium tuberculosisAnti-Infective AgentsDrug Resistance Multiple BacterialRNA Ribosomal 16SmedicineHumansTuberculosisDeoxyribonucleases Type II Site-SpecificMolecular BiologyEthambutolPolymorphism Single-Stranded ConformationalAntibacterial agentGeneticsbiologyPoint mutationSingle-strand conformation polymorphismGeneral MedicineMycobacterium tuberculosisSequence Analysis DNAbiology.organism_classificationMolecular biologyStreptomycinStreptomycinEthambutolmedicine.drugResearch in microbiology
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Concomitant loss of conformation and superantigenic activity of staphylococcal enterotoxin B deletion mutant proteins.

1993

The T-cell-stimulating activity of staphylococcal enterotoxin B (SEB) is an important factor in the pathogenesis of certain staphylococcal diseases. To investigate the immunologically active domains of the SEB molecule, we have produced truncated fragments of recombinant SEB by C-terminal and N-terminal deletions. The fragments were expressed as fusion proteins with protein A, including a cleavage site to remove the protein A part. Mutant proteins were tested for the ability to stimulate human resting T cells and SEB-reactive T-cell clones. Deletion of only 9 amino acids from the C terminus leads to complete loss of T-cell-stimulating activity. Removing further amino acids from the SEB mole…

DNA BacterialStaphylococcus aureusRecombinant Fusion ProteinsImmunologyMutantMolecular Sequence DataBiologyMicrobiologyEpitopeEnterotoxinsMiceStructure-Activity RelationshipMutant proteinAnimalsAmino Acid SequencePeptide sequencechemistry.chemical_classificationAntigens BacterialMice Inbred BALB CBase SequenceC-terminusFusion proteinMolecular biologyAmino acidInfectious DiseaseschemistryMutationParasitologyGene DeletionConformational epitopeResearch Article
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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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Cloning and expression of a cDNA copy of the viral K28 killer toxin gene in yeast

1995

The killer toxin K28, secreted by certain killer strains of the yeast Saccharomyces cerevisiae is genetically encoded by a 1.9 kb double-stranded RNA, M-dsRNA (M28), that is present within the cell as a cytoplasmically inherited virus-like particle (VLP). For stable maintenance and replication, M28-VLPs depend on a second dsRNA virus (LA), which has been shown to encode the major capsid protein (cap) and a capsid-polymerase fusion protein (cap-pol) that provides the toxin-coding M-satellites with their transcription and replicase functions. K28 toxin-coding M28-VLPs were isolated, purified and used in vitro for the synthesis of the single-stranded M28 transcript, which was shown to be of pl…

DNA ComplementarySaccharomyces cerevisiae ProteinsTranscription GeneticMolecular Sequence DataGene ExpressionRNA-dependent RNA polymeraseSaccharomyces cerevisiaeBiologyOpen Reading FramesTranscription (biology)Complementary DNAGene expressionGeneticsAmino Acid SequenceCloning MolecularProtein PrecursorsMolecular BiologyGeneRNA Double-StrandedBase SequenceSequence Analysis RNANucleic acid sequenceRNARNA FungalDNA-Directed RNA PolymerasesSequence Analysis DNAMycotoxinsMolecular biologyKiller Factors YeastOpen reading frameProtein BiosynthesisNucleic Acid ConformationRNA ViralMolecular and General Genetics MGG
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Inverse Conformational Selection in Lipid–Protein Binding

2021

International audience; Interest in lipid interactions with proteins and other biomolecules is emerging not only in fundamental biochemistry but also in the field of nanobiotechnology where lipids are commonly used, for example, in carriers of mRNA vaccines. The outward-facing components of cellular membranes and lipid nanoparticles, the lipid headgroups, regulate membrane interactions with approaching substances, such as proteins, drugs, RNA, or viruses. Because lipid headgroup conformational ensembles have not been experimentally determined in physiologically relevant conditions, an essential question about their interactions with other biomolecules remains unanswered: Do headgroups excha…

DYNAMICSELECTRIC CHARGEBILAYERSPHOSPHATIDYLCHOLINE HEADGROUPMembrane lipidsDEUTERIUMPlasma protein bindingMolecular Dynamics Simulationlipidit010402 general chemistry01 natural sciencesBiochemistrybiomolekyylitCatalysis03 medical and health sciencesMolecular dynamicskemialliset sidoksetColloid and Surface ChemistryProtein structurePHOSPHOLIPID-BINDINGMAGNETIC-RESONANCE[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologySEGMENTAL ORDER[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyConformational ensemblesNuclear Magnetic Resonance Biomolecular030304 developmental biologychemistry.chemical_classification0303 health sciencesChemistryBiomoleculeMEMBRANE-LIPIDSProteinsPhosphatidylglycerolsGeneral Chemistrycomputer.file_formatProtein Data BankLipids0104 chemical sciencesBiophysicsPhospholipid BindingPhosphatidylcholinesMAS NMR1182 Biochemistry cell and molecular biologylipids (amino acids peptides and proteins)proteiinitcomputerProtein Binding
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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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Influence of solvents on conformation of dehydropeptides

2013

Abstract Structural investigations of dehydropeptides containing (Z)-dehydrophenylalanine in solvents characterized by different polarity are discussed. The conformational analysis are based on spectroscopic methods (NMR, CD), molecular modeling techniques and in case of the tripeptide, ab initio methods. The results of temperature experiment indicate, that the only conformation of the investigated hexapeptide 3 is stabilized by intramolecular hydrogen bonds. Depending on the length of the peptide chain, the polarity of solvent influences on arrangement of the side chain of the amino acids or of the main chain of the peptide.

Dehydropeptide conformationchemistry.chemical_classificationCircular dichroismMolecular modelDehydrophenylalanineHydrogen bondStereochemistryOrganic ChemistryAb initioPeptideTripeptideCircular dichroismSolvent polarityNMRAnalytical ChemistryInorganic ChemistrychemistryIntramolecular forceSide chainDehydropeptideSpectroscopyJournal of Molecular Structure
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Conformational analysis of α,β-dehydropeptide models at the HF and DFT levels

2004

Abstract The Ramachandran potential energy surfaces of N-acetyl-α,β-dehydroamino acid N′-monomethylamides Ac-ΔXaa-NHMe (ΔXaa=ΔAla, (Z)-ΔPhe; 1, 2) and N-acetyl-α,β-dehydroamino acid N′,N′-dimethylamides Ac-ΔXaa-NMe2 (ΔXaa=ΔAla, (Z)-ΔPhe, (Z)-ΔAbu; 3–5) were calculated at the HF/6-31G*//HF/3-21G level. The conformers localised were fully optimised at the DFT/B3LYP/6-31+G** level and their relative stabilities were analysed in terms of both π-conjugation and internal hydrogen bonding. The Ac-ΔXaa-NMe2 molecules reveal the low-energy conformer H/F, φ=−41±4°, ψ=128±4°, which is not too easily accessible for common amino acid residues. This conformer is stabilised by the bifurcated N2–CH3 O1 int…

DehydrophenylalanineHydrogen bondStereochemistryIntermolecular forceIntramolecular hydrogen bondingPotential energy surfaceCondensed Matter PhysicsDehydroalanineBiochemistryPotential energyDimethylamideschemistry.chemical_compoundchemistryDehydroalaninePotential energy surfaceMoleculePhysical and Theoretical ChemistryConformational isomerismRamachandran plotJournal of Molecular Structure: THEOCHEM
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