Search results for "Biophysic Al Simulations"

showing 2 items of 2 documents

Construction of Chimeric Dual-Chain Avidin by Tandem Fusion of the Related Avidins

2011

BackgroundAvidin is a chicken egg-white protein with high affinity to vitamin H, also known as D-biotin. Many applications in life science research are based on this strong interaction. Avidin is a homotetrameric protein, which promotes its modification to symmetrical entities. Dual-chain avidin, a genetically engineered avidin form, has two circularly permuted chicken avidin monomers that are tandem-fused into one polypeptide chain. This form of avidin enables independent modification of the two domains, including the two biotin-binding pockets; however, decreased yields in protein production, compared to wt avidin, and complicated genetic manipulation of two highly similar DNA sequences i…

Macromolecular Assemblieslcsh:MedicineBiosensing TechniquesPolymerase Chain ReactionBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureBiotinMacromolecular Structure AnalysisProtein biosynthesisBiomacromolecule-Ligand InteractionsSurface plasmon resonancelcsh:Science0303 health sciencesMultidisciplinarybiologyrespiratory systemRecombinant ProteinsBiochemistryBiotinylationChromatography GelBiophysic Al SimulationsResearch ArticleProtein StructureStructural similarityRecombinant Fusion Proteins030303 biophysicsBiophysicsBiotinMolecular Dynamics SimulationBiokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biology03 medical and health sciencesstomatognathic systemDefense ProteinsEscherichia coliAnimalsGene familyProtein InteractionsBiology030304 developmental biologylcsh:RProteinsComputational BiologySurface Plasmon ResonanceAvidinchemistrySmall MoleculesFermentationbiology.proteinlcsh:QChickensAvidinPLoS ONE
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Conformational changes in acetylcholine binding protein investigated by temperature accelerated molecular dynamics.

2014

Despite the large number of studies available on nicotinic acetylcholine receptors, a complete account of the mechanistic aspects of their gating transition in response to ligand binding still remains elusive. As a first step toward dissecting the transition mechanism by accelerated sampling techniques, we study the ligand-induced conformational changes of the acetylcholine binding protein (AChBP), a widely accepted model for the full receptor extracellular domain. Using unbiased Molecular Dynamics (MD) and Temperature Accelerated Molecular Dynamics (TAMD) simulations we investigate the AChBP transition between the apo and the agonist-bound state. In long standard MD simulations, both confo…

Nicotinic Acetylcholine ReceptorsProtein ConformationGatingMolecular DynamicsLigandsBiochemistryBiophysics SimulationsIon ChannelsMolecular dynamicsAcetylcholine bindingComputational ChemistryBiochemical SimulationsNicotinic AgonistsBiomacromolecule-Ligand InteractionsBiochemistry SimulationsMultidisciplinaryHydrogen bondChemistryPhysicsQTemperatureRLigand (biochemistry)nicotinic receptor molecular dynamics tamd acethylcholine binding proteinChemistryNicotinic agonistBiochemistryMedicineBiophysic Al SimulationsResearch ArticleProtein BindingProtein subunitScienceBiophysicsMolecular Dynamics SimulationProtein ChemistryStatistical MechanicsChemical BiologyAnimalsBiologyAcetylcholine receptorBinding SitesProteinsComputational BiologyHydrogen BondingSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein SubunitsMolluscaAcetylcholine ReceptorsBiophysicsLobelineCarrier ProteinsPLoS ONE
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