Search results for "Static Electricity"

showing 8 items of 98 documents

Energy interactions in amyloid-like fibrils from NNQQNY.

2014

We use large-scale MP2 calculations to analyze the interactions appearing in amyloid fibers, which are difficult to determine experimentally. To this end, dimers and trimers of the hexapeptide NNQQNY from the yeast prion-like protein Sup35 were considered as model systems. We studied the energy interactions present in the three levels of organization in which the formation of amyloid fibrils is structured. The structural changes in the hydrogen bonds were studied too. It was found that the most energetic process is the formation of the β-sheet, which is equally due to both hydrogen bonds and van der Waals interactions. The aromatic rings help stabilize these aggregates through stacking of t…

Steric effectschemistry.chemical_classificationAmyloidHydrogen bondChemistryStereochemistryStatic ElectricityStackingGeneral Physics and AstronomyAromaticityHydrogen BondingRing (chemistry)London dispersion forceProtein Structure SecondaryPolymerizationsymbols.namesakeCrystallographysymbolsNon-covalent interactionsThermodynamicsAmino Acid SequencePhysical and Theoretical Chemistryvan der Waals forceDimerizationPhysical chemistry chemical physics : PCCP
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Improvement of charge-transfer indices for multifunctional amino acids: Application to lysozyme

2008

Valence topological Charge-Transfer (CT) indices are applied to the calculation of pH at the isoelectric point (pI). The model is generalized for molecules with heteroatoms. The ability of the indices for the description of molecular charge distribution is established by comparing them with the pI of 21 amino acids. Linear correlation models are obtained. The CT indices improve multivariable regression equations for pI. The variance decreases by 95%. No superimposition of the corresponding G(k)-J(k) and G(k)(V)-J(k)(V) pairs is observed in most fits, which diminishes the risk of collinearity. The inclusion of heteroatoms in pi-electron system is beneficial for the description of pI, the bec…

Steric effectschemistry.chemical_classificationValence (chemistry)ChemistryStereochemistryStatic ElectricityHeteroatomCharge densityBioengineeringGeneral MedicineHydrogen-Ion ConcentrationAmino acidCrystallographychemistry.chemical_compoundIsoelectric pointModels ChemicalDrug DiscoveryPiMolecular MedicineMuramidaseIsoelectric PointAmino AcidsLysozymeSAR and QSAR in Environmental Research
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Computer Simulations of the Electric Interactions between the Phospholipid Head-Groups and Ionic Admixtures in the Membrane Surface

2001

Some phospholipids (e.g. lecithin) form a system of electric dipoles on the membrane surface layer. In the case of lecithin the positive dipole charge is located on the choline and the negative one on the phosphoric molecule group. These dipoles are arranged almost parallel to the membrane surface. Taking the dipole membrane structure as a base for further investigations, a computer model of the electrostatic interaction between the dipole system and the ionic admixture was investigated. The model presumes hexagonal centered or a rectangular flat geometry of the 121 dipoles distribution. The dipoles may rotate freely around round the motionless symmetry axis perpendicular to the system surf…

Thermodynamic equilibriumChemistryLipid BilayersStatic ElectricityBinding energyAnalytical chemistryIonic bondingCharge (physics)Models TheoreticalModels BiologicalMolecular physicsGeneral Biochemistry Genetics and Molecular BiologyIonKineticsElectric dipole momentDipolePhosphatidylcholinesThermodynamicsMoleculeComputer SimulationPhospholipidsZeitschrift für Naturforschung C
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Interaction of Charged Amino-Acid Side Chains with Ions: An Optimization Strategy for Classical Force Fields

2014

Many well-established classical biomolecular force fields, fitted on the solvation properties of single ions, do not necessarily describe all the details of ion pairing accurately, especially for complex polyatomic ions. Depending on the target application, it might not be sufficient to reproduce the thermodynamics of ion pairing, but it may also be necessary to correctly capture structural details, such as the coordination mode. In this work, we analyzed how classical force fields can be optimized to yield a realistic description of these different aspects of ion pairing. Given the prominent role of the interactions of negatively charged amino-acid side chains and divalent cations in many …

Work (thermodynamics)Static ElectricityAcetatesMolecular Dynamics SimulationIonsymbols.namesakeMolecular dynamicsEngineeringMaterials ChemistryAmino AcidsPhysical and Theoretical ChemistryIonsHydrogen bondChemistryPolyatomic ionSolvationWaterHydrogen BondingCalcium CompoundsSurfaces Coatings and FilmsChemical physicsYield (chemistry)Physical SciencesChemical SciencessymbolsThermodynamicsAtomic physicsvan der Waals forceThe Journal of Physical Chemistry B
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Force probe measurements of antibody-antigen interactions.

2000

The surface force apparatus has been used to quantify directly the forces that govern the interactions between proteins and ligands. In this work, we describe the measured interactions between the antigen fluorescein and the Fab' fragment of the monoclonal 4-4-20 anti-fluorescyl IgG antibody. Here we first describe the use of the surface force apparatus to demonstrate directly the impact of the charge composition in the region of the antibody binding site on the antibody interactions. Several approaches are described for immobilizing antigens, antibodies, and proteins in general for direct force measurements. The measured force profiles presented are accompanied by an extensive discussion o…

biologyChemistryStereochemistryStatic ElectricityAntibodies MonoclonalSurface forces apparatusAdhesionGeneral Biochemistry Genetics and Molecular BiologyAntigen-Antibody Reactionschemistry.chemical_compoundImmunoglobulin Fab FragmentsAntigenStatic electricityAntibody InteractionsAntibody antigenbiology.proteinBiophysicsFluoresceinAntibodyMolecular BiologyMethods (San Diego, Calif.)
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Electrospray ion mobility mass spectrometry of positively charged sodium bis[2-ethythexyl)sulfosuccinate aggregates.

2014

Collision cross-sections (CCS) of positively singly and multiply charged aggregates of the surfactant sodium bis(2-ethylhexyl)sulfosuccinate (AOTNa) in the gas phase have been measured by quadrupole ion mobility time-of-flight mass spectrometry. Calibration of the observed drift times to the CCS of the AOTNa non-covalent aggregates was achieved by collecting, under the same experimental conditions, the drift times of a range of singly and multiply charged polyalanine peptides whose CCS had been obtained by conventional ion mobility spectrometry. Together with an obvious increase of the aggregate cross-section with the aggregation number, it was found that the aggregate cross-section increa…

chemistry.chemical_classificationModels MolecularElectrosprayRange (particle radiation)Dioctyl Sulfosuccinic AcidSpectrometry Mass Electrospray IonizationAggregation numberIon-mobility spectrometrySodiumStatic ElectricityAnalytical chemistrychemistry.chemical_elementIon mobility surfactants AOT collision cross section mass spectrometry supramolecular aggregatesGeneral MedicineMass spectrometryAtomic and Molecular Physics and OpticsIonchemistryModels ChemicalComputer SimulationCounterionSpectroscopyEuropean journal of mass spectrometry (Chichester, England)
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Intra-Helical Salt Bridge Contribution to Membrane Protein Insertion.

2021

ABSTRACTSalt bridges between negatively (D, E) and positively charged (K, R, H) amino acids play an important role in protein stabilization. This has a more prevalent effect in membrane proteins where polar amino acids are exposed to a very hydrophobic environment. In transmembrane (TM) helices the presence of charged residues can hinder the insertion of the helices into the membrane. This can sometimes be avoided by TM region rearrangements after insertion, but it is also possible that the formation of salt bridges could decrease the cost of membrane integration. However, the presence of intra-helical salt bridges in TM domains and their effect on insertion has not been properly studied ye…

chemistry.chemical_classificationProtein Conformation alpha-HelicalCell MembraneStatic ElectricityMembrane ProteinsElectrostaticsTransmembrane proteinAmino acidMembraneMembrane proteinchemistryStructural BiologyBiophysicsSalt bridgeProtein stabilizationAmino AcidsMolecular BiologyHydrophobic and Hydrophilic InteractionsBiogenesisJournal of molecular biology
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Amphoteric, prevailingly cationic L-arginine polymers of poly(amidoamino acid) structure: Synthesis, acid/base properties and preliminary cytocompati…

2013

A linear amphoteric poly(amidoamino acid), L-ARGO7, is prepared by Michael-type polyaddition of L-arginine with N,N′-methylenebisacrylamide. Chain-extension of acrylamide end-capped L-ARGO7 oligomers with piperazine leads to high-molecular-weight copolymers in which L-arginine maintains its absolute configuration. Acid/base properties of L-ARGO7 polymers show isolectric points of ≈10 and positive net average charges per repeating unit at pH = 7.4 from 0.25 to 0.40. These arginine-rich synthetic polymers possibly share some of the unique biological properties of polyarginine cell-permeating peptides. In vitro tests with mouse embryo fibroblasts balb/3T3 clone A31 show that L-ARGO7 polymers a…

poly(amidoamine)Materials Chemistry2506 Metals and AlloyAcrylamidesCell Membrane PermeabilityPolymers and PlasticCell SurvivalL -arginine polymerMedicine (all)Static ElectricityBioengineeringHydrogen-Ion ConcentrationArgininebiological application of polymerBiomaterialPiperazinesMicebiocompatibilityNIH 3T3 CellsPolyaminesAnimalsIsoelectric Pointpoly(amidoamino acid)PeptidesHydrophobic and Hydrophilic InteractionsBiotechnology
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