Search results for "Biomolecule"

showing 10 items of 666 documents

Orientational landscapes of peptides in membranes: prediction of (2)H NMR couplings in a dynamic context.

2009

Unlike soluble proteins, membrane polypeptides face an anisotropic milieu. This imposes restraints on their orientation and provides a reference that makes structure prediction tractable by minimalistic thermodynamic models. Here we use this framework to build orientational distributions of monomeric membrane-bound peptides and to predict their expected solid-state (2)H NMR quadrupolar couplings when labeled at specific side chain positions. Using a complete rigid-body sampling of configurations relative to an implicit lipid membrane, peptide free energy landscapes are calculated. This allows us to obtain probability distributions of the peptide tilt, azimuthal rotation, and depth of membra…

Models MolecularMagnetic Resonance SpectroscopyMembrane FluidityPopulationDegrees of freedom (physics and chemistry)Context (language use)BiochemistryQuantitative Biology::Subcellular ProcessesComputational chemistryOrientation (geometry)Computer SimulationLipid bilayereducationAnisotropyPhysics::Biological PhysicsQuantitative Biology::Biomoleculeseducation.field_of_studyChemistryCell MembraneMaxima and minimaMembraneSolubilityChemical physicsThermodynamicsPeptidesAlgorithmsBiochemistry
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Atomic Mean-Square Displacements in Proteins by Molecular Dynamics: A Case for Analysis of Variance

2004

AbstractInformation on protein internal motions is usually obtained through the analysis of atomic mean-square displacements, which are a measure of variability of the atomic positions distribution functions. We report a statistical approach to analyze molecular dynamics data on these displacements that is based on probability distribution functions. Using a technique inspired by the analysis of variance, we compute unbiased, reliable mean-square displacements of the atoms and analyze them statistically. We applied this procedure to characterize protein thermostability by comparing the results for a thermophilic enzyme and a mesophilic homolog. In agreement with previous experimental observ…

Models MolecularMean squareSurface (mathematics)Hot TemperatureTime FactorsNitrogenProtein ConformationMolecular ConformationBiophysicsBiophysical Theory and ModelingMeasure (mathematics)Protein Structure SecondaryMolecular dynamicsBacterial ProteinsStatistical physicsProbabilityThermostabilityAnalysis of VarianceQuantitative Biology::BiomoleculesModels StatisticalChemistryProteinsModels TheoreticalCrystallographyDistribution functionSolventsProbability distributionAnalysis of varianceAlgorithms
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How molecular knots can pass through each other

2014

We propose a mechanism in which two molecular knots pass through each other and swap positions along a polymer strand. Associated free energy barriers in our simulations only amount to a few $k_{B}T$, which may enable the interchange of knots on a single DNA strand.

Models MolecularMultidisciplinaryComputersPolymersChemistryFOS: Physical sciencesBiomolecules (q-bio.BM)DNACondensed Matter - Soft Condensed MatterMolecular physicsNanostructuresDiffusionMolecular dynamicsCrystallographyQuantitative Biology - BiomoleculesBiological Physics (physics.bio-ph)FOS: Biological sciencesPhysical SciencesNucleic Acid ConformationThermodynamicsSoft Condensed Matter (cond-mat.soft)Physics - Biological Physics
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The Role of Adenine Excimers in the Photophysics of Oligonucleotides

2009

Energies and structures of different arrangements of the stacked adenine homodimer have been computed at the ab initio CASPT2 level of theory in isolation and in an aqueous environment. Adenine dimers are shown to form excimer singlet states with different degrees of stacking and interaction. A model for a 2-fold decay dynamics of adenine oligomers can be supported in which, after initial excitation in the middle UV range, unstacked or slightly stacked pairs of nucleobases will relax by an ultrafast internal conversion to the ground state, localizing the excitation in the monomer and through the corresponding conical intersection with the ground state. On the other hand, long-lifetime intra…

Models MolecularPhotochemistryUltraviolet RaysMolecular ConformationOligonucleotidesAb initioPhotochemistryExcimerBiochemistryCatalysisNucleobaseColloid and Surface ChemistryUltrafast laser spectroscopySinglet stateQuantitative Biology::BiomoleculesChemistryAdenineDNAGeneral ChemistryConical intersectionInternal conversion (chemistry)Chemical physicsNucleic Acid ConformationSpectrophotometry UltravioletGround stateDimerizationHydrogenJournal of the American Chemical Society
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Trimeric HIV Env provides epitope occlusion mediated by hypervariable loops

2014

AbstractHypervariable loops of HIV-1 Env protein gp120 are speculated to play roles in the conformational transition of Env to the receptor binding-induced metastable state. Structural analysis of full-length Env-based immunogens, containing the entire V2 loop, displayed tighter association between gp120 subunits, resulting in a smaller trimeric diameter than constructs lacking V2. A prominent basal quaternary location of V2 and V3′ that challenges previous reports would facilitate gp41-independent gp120-gp120 interactions and suggests a quaternary mechanism of epitope occlusion facilitated by hypervariable loops. Deletion of V2 resulted in dramatic exposure of basal, membrane-proximal gp41…

Models MolecularProtein ConformationvirusesHuman immunodeficiency virus (HIV)[CHIM.THER]Chemical Sciences/Medicinal ChemistryPlasma protein bindingHIV Envelope Protein gp120medicine.disease_causeEnv ProteinEpitopeenv Gene ProductsEpitopesProtein structureModelsComputingMilieux_MISCELLANEOUSSequence DeletionGeneticsMultidisciplinary[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Transition (genetics)biologyenv Gene Products Human Immunodeficiency Virusvirus diseaseshypervariable loopsHIV Envelope Protein gp41[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]3. Good health[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]CD4 AntigensHIV/AIDSAntibodyHuman Immunodeficiency VirusProtein BindingEnvGp41ArticleVaccine RelatedGenetics[CHIM.CRIS]Chemical Sciences/CristallographymedicineHumansProtein Interaction Domains and Motifs[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]AntigensVaccine Related (AIDS)Preventionta1182Molecular[SDV.IMM.IMM]Life Sciences [q-bio]/Immunology/ImmunotherapyCD4Peptide Fragmentsgp120Good Health and Well BeingHIV-1biology.proteinImmunizationProtein MultimerizationproteinScientific Reports
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Irreversible gelation of thermally unfolded proteins:structural and mechanical properties of lysozyme aggregates

2010

The formation of protein aggregates is important in many fields of life science and technology. The morphological and mechanical properties of protein solutions depend upon the molecular conformation and thermodynamic and environmental conditions. Non-native or unfolded proteins may be kinetically trapped into irreversible aggregates and undergo precipitation or gelation. Here, we study the thermal aggregation of lysozyme in neutral solutions. We characterise the irreversible unfolding of lysozyme by differential scanning calorimetry. The structural properties of aggregates and their mechanisms of formation with the eventual gelation are studied at high temperature by spectroscopic, rheolog…

Models MolecularProtein FoldingCircular dichroismGelationProtein ConformationDiffusionBiophysicsProtein aggregationUnfoldingchemistry.chemical_compoundDifferential scanning calorimetryProtein structureAnimalsQuantitative Biology::BiomoleculesChemistryPrecipitation (chemistry)Circular DichroismTemperaturePercolationGeneral MedicineBlood Coagulation FactorsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Thermal irreversibilityCrystallographyChemical physicsThermodynamicsMuramidaseProtein foldingLysozymeProtein aggregation
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ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space.

2015

Molecular machines or macromolecular complexes are supramolecular assemblies of biomolecules that ensure cellular homeostasis. Structure determination of those complexes in a purified state is often a tedious undertaking due to the compositional complexity and the related relative structural instability. To improve the stability of macromolecular complexes in vitro, we present here a generic method that optimizes the stability, homogeneity and solubility of macromolecular complexes by sparse-matrix screening of their thermal unfolding behaviour in the presence of various buffers and small molecules. The method includes the automated analysis of thermal unfolding curves based on a newly deve…

Models MolecularProtein FoldingProtein ConformationSupramolecular chemistryBiochemistryArticleProtein structureComputer SimulationMolecular Biologychemistry.chemical_classificationBinding SitesBiomoleculeMolecular biophysicsCell BiologyMolecular machineChemical spacechemistryModels ChemicalChemical physicsMultiprotein ComplexesBiophysicsProtein foldingCrystallizationAlgorithmsSoftwareBiotechnologyMacromoleculeProtein BindingNature methods
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Novel 3D bio-macromolecular bilinear descriptors for protein science: Predicting protein structural classes

2015

In the present study, we introduce novel 3D protein descriptors based on the bilinear algebraic form in the ℝn space on the coulombic matrix. For the calculation of these descriptors, macromolecular vectors belonging to ℝn space, whose components represent certain amino acid side-chain properties, were used as weighting schemes. Generalization approaches for the calculation of inter-amino acidic residue spatial distances based on Minkowski metrics are proposed. The simple- and double-stochastic schemes were defined as approaches to normalize the coulombic matrix. The local-fragment indices for both amino acid-types and amino acid-groups are presented in order to permit characterizing fragme…

Models MolecularProtein structural classesMathematical parametersProtein functionQuantitative Structure-Activity RelationshipBilinear interpolationQuantitative structure activity relation3D protein descriptorBilinear formProceduresChemical structureStatistical parametersMinkowski spaceProtein analysisAmino AcidsPriority journalMathematicsInterpretabilityQuantitative Biology::BiomoleculesApplied MathematicsStatistical parameterValidation studyGeneral MedicineComputer simulationDiscriminant analysisReproducibilityAmino acidAlgorithmChemistryProtein conformationModeling and SimulationStatistical modelGeneral Agricultural and Biological SciencesBiological systemAmino acid analysisAlgorithmsNonbiological modelStatistics and ProbabilityCorrelation coefficientLDAMacromolecular SubstancesMarkov chainMacromoleculeStructure analysisModels BiologicalArticleGeneral Biochemistry Genetics and Molecular BiologyCombinatoricsStochastic processesBilinear formBiologyMatrixGeneral Immunology and MicrobiologyProteinCoulombic matrixComputational BiologyProteinsReproducibility of ResultsLinear discriminant analysisWeightingCorrelation coefficientProtein structureBiological modelLinear ModelsThree-dimensional modelingJournal of Theoretical Biology
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Calculation of partition coefficient and hydrophobic moment of the secondary structure of lysozyme

2001

A method that permits a semiquantitative estimate of the partitioning of any solute between any two media is presented. As an example, the partition coefficients and hydrophobic moment of the secondary structure of lysozyme are calculated. Program GSCAP is written as a version of Pascal's solvent-dependent conformational analysis (SCAP) program. The dipole moments calculated for the helices are trebled with respect to that for the sheet. For helices, the main contribution to the water-accessible surface area is the hydrophobic term, while the hydrophilic part dominates in the sheet. Molecular globularity and the three studied partition coefficients differentiate between helices and sheet.

Models MolecularQuantitative Biology::BiomoleculesChromatographyOrganic ChemistrySolvationGeneral MedicineBiochemistryProtein Structure SecondaryAnalytical ChemistryGibbs free energyCondensed Matter::Soft Condensed MatterPartition coefficientchemistry.chemical_compoundsymbols.namesakeDipolechemistrysymbolsThermodynamicsMoleculeMuramidaseLysozymeProtein secondary structureJournal of Chromatography A
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Canonical azimuthal rotations and flanking residues constrain the orientation of transmembrane helices.

2013

AbstractIn biological membranes the alignment of embedded proteins provides crucial structural information. The transmembrane (TM) parts have well-defined secondary structures, in most cases α-helices and their orientation is given by a tilt angle and an azimuthal rotation angle around the main axis. The tilt angle is readily visualized and has been found to be functionally relevant. However, there exist no general concepts on the corresponding azimuthal rotation. Here, we show that TM helices prefer discrete rotation angles. They arise from a combination of intrinsic properties of the helix geometry plus the influence of the position and type of flanking residues at both ends of the hydrop…

Models MolecularQuantitative Biology::BiomoleculesPotassium ChannelsRotationChemistryCell MembraneMolecular Sequence DataBiophysicsMembraneMembrane ProteinsBiological membraneRotationTransmembrane proteinPeptide FragmentsProtein Structure SecondaryCore (optical fiber)CrystallographyTransmembrane domainChemical physicsOrientation (geometry)HelixPolarAmino Acid SequenceProtein MultimerizationProtein Structure QuaternaryBiophysical journal
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