Search results for "conformation"

showing 10 items of 1414 documents

Fine-tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin-type peptidyl prolyl isomerases

2017

AbstractParvulins or rotamases form a distinct group within peptidyl prolyl cis-trans isomerases. Their exact mode of action as well as the role of conserved residues in the family are still not unambiguously resolved. Using backbone S2 order parameters and NOEs as restraints, we have generated dynamic structural ensembles of three distinct parvulins, SaPrsA, TbPin1 and CsPinA. The resulting ensembles are in good agreement with the experimental data but reveal important differences between the three enzymes. The largest difference can be attributed to the extent of the opening of the substrate binding cleft, along which motional mode the three molecules occupy distinct regions. Comparison w…

0301 basic medicineFine-tuningentsyymitStaphylococcus aureusparvulinsProtein ConformationParvulinenzymesTrypanosoma brucei bruceibinding cleftIsomeraseisomerasesArticleWW domain03 medical and health sciencesHumansAmino Acid SequenceMode of actionta116Multidisciplinary030102 biochemistry & molecular biologybiologyChemistryDynamics (mechanics)ta1182Peptidylprolyl IsomeraseArchaeaNIMA-Interacting Peptidylprolyl Isomerase030104 developmental biologyOrder (biology)PIN1Biophysicsbiology.proteinProtein BindingScientific Reports
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Direct observation of alpha-lactalbumin, adsorption and incorporation into lipid membrane and formation of lipid/protein hybrid structures

2019

The interaction between proteins and membranes is of great interest in biomedical and biotechnological research for its implication in many functional and dysfunctional processes. We present an experimental study on the interaction between model membranes and alpha-lactalbumin (alpha-La). alpha-La is widely studied for both its biological function and its anti-tumoral properties. We use advanced fluorescence microscopy and spectroscopy techniques to characterize alpha-La-membrane mechanisms of interaction and alpha-La-induced modifications of membranes when insertion of partially disordered regions of protein chains in the lipid bilayer is favored. Moreover, using fluorescence lifetime imag…

0301 basic medicineFluorescence-lifetime imaging microscopyProtein ConformationLipid BilayersBiophysics02 engineering and technologyBiochemistryMembrane Lipids03 medical and health sciencesProtein structureMembrane fluidityFluorescence microscopeAnimalsHumansLipid bilayerMolecular BiologyFluorescent DyesChemistryMembrane structure021001 nanoscience & nanotechnologyLipids2-PHOTON FLUORESCENCE MICROSCOPY; MOLTEN GLOBULE STATE; PARTIALLY FOLDED CONFORMATIONS; PROTEIN INTERACTIONS; CIRCULAR-DICHROISM; AMPHITROPIC PROTEINS; AMYLOID AGGREGATION; PHASOR APPROACH; OLEIC-ACID; LAURDANSpectrometry Fluorescence030104 developmental biologyMembranefluorescence FLIM Protein membrane interaction IDPLactalbuminBiophysicsCattleAdsorption0210 nano-technologyProtein adsorptionBiochimica et Biophysica Acta (BBA) - General Subjects
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Access to new highly potent antileukemia, antiviral and antimalarial agents via hybridization of natural products (homo)egonol, thymoquinone and arte…

2018

Hybridization of natural products has high potential to further improve their activities and may produce synergistic effects between linked pharmacophores. Here we report synthesis of nine new hybrids of natural products egonol, homoegonol, thymoquinone and artemisinin and evaluation of their activities against P. falciparum 3D7 parasites, human cytomegalovirus, sensitive and multidrug-resistant human leukemia cells. Most of the new hybrids exceed their parent compounds in antimalarial, antiviral and antileukemia activities and in some cases show higher in vitro efficacy than clinically used reference drugs chloroquine, ganciclovir and doxorubicin. Combined, our findings stress the high pot…

0301 basic medicineGanciclovirCell SurvivalPlasmodium falciparumClinical BiochemistryMolecular ConformationCytomegalovirusPharmaceutical ScienceAntineoplastic AgentsAnisolesPharmacologyCrystallography X-RayAntiviral Agents01 natural sciencesBiochemistryAntimalarials03 medical and health scienceschemistry.chemical_compoundChloroquineCell Line TumorDrug DiscoveryBenzoquinonesmedicineAnimalsHumansPotencyDoxorubicinAntimalarial AgentArtemisininMolecular BiologyThymoquinoneBenzofuransBiological Products010405 organic chemistryChemistryOrganic ChemistryArtemisinins0104 chemical sciences030104 developmental biologyMolecular MedicinePharmacophoremedicine.drugBioorganic & Medicinal Chemistry
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CLOVE: classification of genomic fusions into structural variation events

2017

Background A precise understanding of structural variants (SVs) in DNA is important in the study of cancer and population diversity. Many methods have been designed to identify SVs from DNA sequencing data. However, the problem remains challenging because existing approaches suffer from low sensitivity, precision, and positional accuracy. Furthermore, many existing tools only identify breakpoints, and so not collect related breakpoints and classify them as a particular type of SV. Due to the rapidly increasing usage of high throughput sequencing technologies in this area, there is an urgent need for algorithms that can accurately classify complex genomic rearrangements (involving more than …

0301 basic medicineGenomicsBiologycomputer.software_genrelcsh:Computer applications to medicine. Medical informaticsBiochemistryChromosomesDNA sequencingSet (abstract data type)Structural variationUser-Computer Interface03 medical and health sciencesStructural BiologyEscherichia coliHumansCopy-number variationMolecular Biologylcsh:QH301-705.5InternetMethodology ArticleApplied MathematicsBreakpointGenomic rearrangementsDNAGenomicsStructural variationsComputer Science ApplicationsIdentification (information)030104 developmental biologylcsh:Biology (General)Nucleic Acid ConformationGraph (abstract data type)lcsh:R858-859.7Data miningcomputerAlgorithmsBMC Bioinformatics
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Synthesis, antitumor activity and CDK1 inhibiton of new thiazole nortopsentin analogues

2017

A new series of thiazole nortopsentin analogues was conveniently synthesized with fair overall yields. The antiproliferative activity of the new derivatives was tested against different human tumor cell lines of the NCI full panel. Four of them showed good antitumor activity with GI(50) values from micro to nanomolar level. The mechanism of the antiproliferative effect of these derivatives, was pro-apoptotic, being associated with externalization of plasma membrane phosphatidylserine and DNA fragmentation. The most active and selective of the new thiazoles confined viable cells in G2/M phase and markedly inhibited in vitro CDK1 activity. (C) 2017 Elsevier Masson SAS.

0301 basic medicineIndolesCell SurvivalStereochemistryMolecular ConformationNortopsentin analogues3-b]pyridinesAntineoplastic AgentsApoptosisMarine alkaloids Nortopsentin analogues Antiproliferative activity Apoptosis CDK1 inhibitors Thiazolyl-1H-pyrrolo[23-b]pyridinesAntiproliferative activity01 natural sciencesStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundMarine alkaloidsCDC2 Protein KinaseDrug DiscoveryHumansThiazoleProtein Kinase InhibitorsCell ProliferationPharmacologyCyclin-dependent kinase 1Dose-Response Relationship DrugMarine alkaloids; Nortopsentin analogues; Antiproliferative activity; Apoptosis; CDK1 inhibitors; Thiazolyl-1H-pyrrolo[2; 3-b]pyridines010405 organic chemistryOrganic ChemistryImidazolesGeneral MedicinePhosphatidylserineThiazolyl-1H-pyrrolo[2Settore CHIM/08 - Chimica FarmaceuticaCyclin-Dependent KinasesIn vitro0104 chemical sciencesCDK1 inhibitors030104 developmental biologyMembranechemistryCell cultureApoptosisMCF-7 CellsDNA fragmentationCaco-2 CellsDrug Screening Assays Antitumor
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In Silico Insights towards the Identification of NLRP3 Druggable Hot Spots

2019

NLRP3 (NOD-like receptor family, pyrin domain-containing protein 3) activation has been linked to several chronic pathologies, including atherosclerosis, type-II diabetes, fibrosis, rheumatoid arthritis, and Alzheimer’s disease. Therefore, NLRP3 represents an appealing target for the development of innovative therapeutic approaches. A few companies are currently working on the discovery of selective modulators of NLRP3 inflammasome. Unfortunately, limited structural data are available for this target. To date, MCC950 represents one of the most promising noncovalent NLRP3 inhibitors. Recently, a possible region for the binding of MCC950 to the NLRP3 protein was described but no details were …

0301 basic medicineInflammasomesComputer sciencehomology modelingMolecular ConformationDruggabilitymcc950Ligands01 natural sciencesPyrin domainlcsh:Chemistrynlrp3 modulationlcsh:QH301-705.5SpectroscopyMolecular Structureintegumentary systemCommunicationInflammasomeGeneral MedicineComputer Science ApplicationsMolecular Docking SimulationdockingProtein Bindingmedicine.drugIn silicoinduced-fit dockingComputational biologyMolecular Dynamics Simulation010402 general chemistryCatalysisInorganic ChemistryStructure-Activity Relationship03 medical and health sciencesNLR Family Pyrin Domain-Containing 3 Proteinnacht domainmedicineHumansHomology modelingPhysical and Theoretical ChemistryMolecular BiologyBinding SitesOrganic ChemistryHydrogen BondingBinding processmolecular dynamics0104 chemical sciences030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Docking (molecular)MutationNACHT domainwalker bInternational Journal of Molecular Sciences
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Chromophore-Protein Interplay During the Phytochrome Photocycle Revealed by Step-Scan FTIR Spectroscopy

2018

Phytochrome proteins regulate many photoresponses of plants and microorganisms. Light absorption causes isomerization of the biliverdin chromophore, which triggers a series of structural changes to activate the signaling domains of the protein. However, the structural changes are elusive, and therefore the molecular mechanism of signal transduction remains poorly understood. Here, we apply two-color step-scan infrared spectroscopy to the bacteriophytochrome from Deinococcus radiodurans. We show by recordings in H2O and D2O that the hydrogen bonds to the biliverdin D-ring carbonyl become disordered in the first intermediate (Lumi-R) forming a dynamic microenvironment, then completely detach …

0301 basic medicineInfrared spectroscopyMolecular Dynamics SimulationBiochemistryCatalysis03 medical and health scienceschemistry.chemical_compoundchromophore-protein interplayColloid and Surface ChemistryBacterial ProteinsSpectroscopy Fourier Transform InfraredPeptide bondta116BiliverdinbiologyPhytochromeHydrogen bondBiliverdineta1182WaterHydrogen BondingDeinococcus radioduransGeneral ChemistryChromophorePhotochemical Processesbiology.organism_classification030104 developmental biologychemistryBiophysicsProtein Conformation beta-StrandDeinococcusPhytochromevalokemiaproteiinitSignal transductionstep-scan FTIR spectroscopyAdenylyl CyclasesJournal of the American Chemical Society
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Correction for Chakroun et al., Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

2016

Entomopathogenic bacteria produce insecticidal proteins that accumulate in inclusion bodies or parasporal crystals (such as the Cry and Cyt proteins) as well as insecticidal proteins that are secreted into the culture medium. Among the latter are the Vip proteins, which are divided into four families according to their amino acid identity. The Vip1 and Vip2 proteins act as binary toxins and are toxic to some members of the Coleoptera and Hemiptera. The Vip1 component is thought to bind to receptors in the membrane of the insect midgut, and the Vip2 component enters the cell, where it displays its ADP-ribosyltransferase activity against actin, preventing microfilament formation. Vip3 has no …

0301 basic medicineInsecticidesInsectaProtein ConformationBacterial ToxinsDrug ResistanceReviewsProtein EngineeringMicrobiology03 medical and health sciencesBacterial ProteinsBotanyTable (landform)AnimalsAmino Acid SequenceAuthor CorrectionPest Control BiologicalMolecular BiologyConserved SequencebiologyBacteriafungibiology.organism_classificationPlants Genetically Modified030104 developmental biologyInfectious DiseasesBacteria
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Conformational dynamics of a single protein monitored for 24 hours at video rate

2018

We use plasmon rulers to follow the conformational dynamics of a single protein for up to 24 h at a video rate. The plasmon ruler consists of two gold nanospheres connected by a single protein linker. In our experiment, we follow the dynamics of the molecular chaperone heat shock protein 90 (Hsp90), which is known to show “open” and “closed” conformations. Our measurements confirm the previously known conformational dynamics with transition times in the second to minute time scale and reveals new dynamics on the time scale of minutes to hours. Plasmon rulers thus extend the observation bandwidth 3–4 orders of magnitude with respect to single-molecule fluorescence resonance energy transfer a…

0301 basic medicineLetterProtein ConformationMolecular ConformationFOS: Physical sciencesHsp90Bioengineeringsingle molecule02 engineering and technology7. Clean energyQuantitative Biology - Quantitative Methods03 medical and health sciencesMolecular dynamicsFluorescence Resonance Energy TransferNanotechnologyGeneral Materials ScienceHSP90 Heat-Shock ProteinsPhysics - Biological PhysicsQuantitative Methods (q-bio.QM)PlasmonPhysicsVideo rateMechanical EngineeringProtein dynamics92Biomolecules (q-bio.BM)General ChemistrySurface Plasmon Resonance021001 nanoscience & nanotechnologyCondensed Matter PhysicsGold nanospheres030104 developmental biologyFörster resonance energy transferQuantitative Biology - BiomoleculesBiological Physics (physics.bio-ph)Chemical physicsFOS: Biological sciencesprotein dynamicsPlasmon rulernonergodicityGold0210 nano-technologyLinker
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19F NMR as a versatile tool to study membrane protein structure and dynamics.

2019

Abstract To elucidate the structures and dynamics of membrane proteins, highly advanced biophysical methods have been developed that often require significant resources, both for sample preparation and experimental analyses. For very complex systems, such as membrane transporters, ion channels or G-protein coupled receptors (GPCRs), the incorporation of a single reporter at a select site can significantly simplify the observables and the measurement/analysis requirements. Here we present examples using 19F nuclear magnetic resonance (NMR) spectroscopy as a powerful, yet relatively straightforward tool to study (membrane) protein structure, dynamics and ligand interactions. We summarize meth…

0301 basic medicineMagnetic Resonance SpectroscopyChemistryCryo-electron microscopyProtein ConformationProtein dynamicsClinical BiochemistryMembrane ProteinsFluorine-19 NMRFluorine010402 general chemistryLigands01 natural sciencesBiochemistry0104 chemical sciences03 medical and health sciences030104 developmental biologyMembraneProtein structureMembrane proteinBiophysicsMolecular BiologyIon channelG protein-coupled receptorProtein BindingBiological chemistry
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