Search results for " secondary"

showing 10 items of 692 documents

Solid state NMR analysis of peptides in membranes: Influence of dynamics and labeling scheme.

2010

The functional state of a membrane-active peptide is often defined by its conformation, molecular orientation, and its oligomeric state in the lipid bilayer. These "static" structural properties can be routinely studied by solid state NMR using isotope-labeled peptides. In the highly dynamic environment of a liquid crystalline biomembrane, however, the whole-body fluctuations of a peptide are also of paramount importance, although difficult to address and most often ignored. Yet it turns out that disregarding such motional averaging in calculating the molecular alignment from orientational NMR-constraints may give a misleading, if not false picture of the system. Here, we demonstrate that t…

Models MolecularLipid BilayersBiophysicsPeptideWhole body fluctuationBiochemistryProtein Structure SecondaryOrientation (geometry)Side chainLipid bilayerNuclear Magnetic Resonance BiomolecularNMR tensor orientationchemistry.chemical_classificationChemistrySolid-state 2H- 19F- 15N-NMRPeptide orientationMembrane ProteinsBiological membraneCell BiologyGALAMembrane-bound peptidePISEMACrystallographyMembraneSolid-state nuclear magnetic resonanceChemical physicsIsotope LabelingHelixIsotope labeling schemeα-helicesPeptide dynamicPeptidesBiochimica et biophysica acta
researchProduct

Influence of Whole-Body Dynamics on 15N PISEMA NMR Spectra of Membrane Proteins: A Theoretical Analysis

2009

AbstractMembrane proteins and peptides exhibit a preferred orientation in the lipid bilayer while fluctuating in an anisotropic manner. Both the orientation and the dynamics have direct functional implications, but motions are usually not accessible, and structural descriptions are generally static. Using simulated data, we analyze systematically the impact of whole-body motions on the peptide orientations calculated from two-dimensional polarization inversion spin exchange at the magic angle (PISEMA) NMR. Fluctuations are found to have a significant effect on the observed spectra. Nevertheless, wheel-like patterns are still preserved, and it is possible to determine the average peptide til…

Models MolecularMagic angleRotationGaussianLipid BilayersNormal DistributionBiophysicsMolecular physicsProtein Structure SecondarySpectral lineQuantitative Biology::Subcellular ProcessesMolecular dynamicssymbols.namesakeNuclear magnetic resonanceOrientationComputer SimulationLipid bilayerAnisotropyNuclear Magnetic Resonance BiomolecularQuantitative Biology::BiomoleculesChemistryMembranePolarization (waves)AmplitudesymbolsDimyristoylphosphatidylcholinePeptidesBiophysical Journal
researchProduct

Backbone dynamics of rusticyanin: the high hydrophobicity and rigidity of this blue copper protein is responsible for its thermodynamic properties.

2003

Local dynamics and solute-solvent exchange properties of rusticyanin (Rc) from Thiobacillus ferrooxidans have been studied by applying heteronuclear ((1)H, (15)N) NMR spectroscopy. (15)N relaxation parameters have been determined for the reduced protein, and a model-free analysis has been applied. The high average value of the generalized order parameter, S(2) (0.93), indicates that Rc is very rigid. The analysis of cross correlation rates recorded in both the reduced and the oxidized forms conclusively proves that Rc possesses the same dynamic features in both oxidation states. The accessibility of backbone amide protons to the solvent at different time scales has also been studied by appl…

Models MolecularMagnetic Resonance SpectroscopyCopper proteinWaterNuclear magnetic resonance spectroscopyThiobacillusBiochemistryProtein Structure SecondaryProtein Structure TertiarySolventMetalchemistry.chemical_compoundCrystallographyProtein structureHeteronuclear moleculechemistryBacterial ProteinsAzurinvisual_artAmideRusticyaninvisual_art.visual_art_mediumThermodynamicsHydrophobic and Hydrophilic InteractionsCopperBiochemistry
researchProduct

Oligonuclear Ferrocene Amides: Mixed‐Valent Peptides and Potential Redox‐Switchable Foldamers

2010

Trinuclear ferrocene tris-amides were synthesized from an Fmoc- or Boc-protected ferrocene amino acid, and hydrogen-bonded zigzag conformations were determined by NMR spectroscopy, molecular modelling, and X-ray diffraction. In these ordered secondary structures orientation of the individual amide dipole moments approximately in the same direction results in a macrodipole moment similar to that of α-helices composed of α-amino acids. Unlike ordinary α-amino acids, the building blocks in these ferrocene amides with defined secondary structure can be sequentially oxidized to mono-, di-, and trications. Singly and doubly charged mixed-valent cations were probed experimentally by Vis/NIR, param…

Models MolecularMagnetic Resonance SpectroscopyMolecular StructureMetallocenesHydrogen bondOrganic ChemistryInorganic chemistryMolecular ConformationGeneral ChemistryNuclear magnetic resonance spectroscopyIntervalence charge transferAmidesCatalysischemistry.chemical_compoundCrystallographyFerrocenechemistryIntramolecular forceAmideMoleculeFerrous CompoundsPeptidesOxidation-ReductionProtein secondary structureChemistry – A European Journal
researchProduct

Synthesis, Structure and Conformation of Partially-Modified Retro- and Retro-Inversoψ[NHCH(CF3)]Gly Peptides

2003

Partially modified retro- (PMR) and retro-inverso (PMRI) psi[NHCH(CF(3))]Gly peptides, a conceptually new class of peptidomimetics, have been synthesized in wide structural diversity and variable length by aza-Michael reaction of enantiomerically pure alpha-amino esters and peptides with enantiomerically and geometrically pure N-4,4,4-trifluorocrotonoyl-oxazolidin-2-ones. The factors underlying the observed moderate to good diastereocontrol have been investigated. The conformations of model PMR-psi[NHCH(CF(3))]Gly tripeptides have been studied in solution by (1)H NMR spectroscopy supported by MD calculations, as well as in the solid-state by X-ray diffraction. Remarkable stability of turn-l…

Models MolecularMagnetic Resonance SpectroscopyMolecular StructureProtein ConformationChemistryStereochemistryHydrogen bondOrganic ChemistryTemperatureReproducibility of ResultsGeneral ChemistryTripeptideCrystal structureCrystallography X-RayBiochemistryProtein Structure SecondaryCatalysisSolutionsModels ChemicalTetrahedral carbonyl addition compoundIntramolecular forceSide chainProton NMRPeptide bondOligopeptidesChemistry - A European Journal
researchProduct

Conformational and structural analysis of the equilibrium between single- and double-strand ?-helix of aD,L-alternating oligonorleucine

2004

Alternating sequences of D and L residues in peptides are directly related to the formation of several kinds of regular helical conformations usually called beta-helices. The major feature of these structures is that they can be associated with the transmembrane ion-conducting channel activity in some natural antibacterial peptides. The study of alternating D,L synthetic peptides is critical to understand how factors such as surrounding media, main chain length, type of side chain and terminal groups, among others, can determine the adoption of a specific kind of beta-helix. Early studies pointed out that the peptides Boc-(D-NLeu-L-NLeu)(6)-D-MeNLe-L-Nl-D-Nl-L-Nl-OMe (Boc: tert-butyloxycarb…

Models MolecularMagnetic Resonance SpectroscopyProtein ConformationStereochemistryDimerMolecular Sequence DataBiophysicsDNA Single-StrandedBeta helixStereoisomerismAntiparallel (biochemistry)BiochemistryProtein Structure SecondaryBiomaterialsMolecular dynamicschemistry.chemical_compoundProtein structureNorleucineSide chainAmino Acid SequenceChemistryOrganic ChemistryStereoisomerismDNAGeneral MedicineNuclear magnetic resonance spectroscopyCrystallographyNucleic Acid ConformationThermodynamicsOligopeptidesBiopolymers
researchProduct

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
researchProduct

Redox-responsive organometallic foldamers from ferrocene amino acid: Solid-phase synthesis, secondary structure and mixed-valence properties

2011

Oligoferrocenes Fmoc-Fca(n)-OMe (n=3-5) are assembled in a stepwise precise manner from Fmoc-protected ferrocene amino acid Fmoc-Fca-OH (H-Fca-OH = 1-amino-1'-ferrocene carboxylic acid; Fmoc = 9-fluorenylmethyloxycarbonyl) via amide bonds on solid supports by sequential Fmoc deprotection, acid activation and coupling steps. The resulting well-defined oligomers form ordered zigzag structures in THF solution with characteristic hydrogen bonding patterns. Electrochemical experiments reveal sequential oxidations of the individual ferrocene units in these peptides giving mixed-valent cations. Optical intervalence electron transfer is detected by intervalence transitions in the near-IR.

Models MolecularMetallocenesStereochemistryCarboxylic acidProtein Structure SecondaryInorganic Chemistrychemistry.chemical_compoundElectron transferSolid-phase synthesisPolymer chemistryOrganometallic CompoundsFerrous CompoundsAmino AcidsProtein secondary structurechemistry.chemical_classificationFluorenesValence (chemistry)Hydrogen bondSpectrum AnalysisDipeptidesAmino acidSolutionschemistryFerrocenePeptidomimeticsOxidation-ReductionDalton Transactions
researchProduct

Peptides Derived from Apoptotic Bax and Bid Reproduce the Poration Activity of the Parent Full-Length Proteins

2005

Bax and Bid are proapoptotic proteins of the Bcl-2 family that regulate the release of apoptogenic factors from mitochondria. Although they localize constitutively in the cytoplasm, their apoptotic function is exerted at the mitochondrial outer membrane, and is related to their ability to form transbilayer pores. Here we report the poration activity of fragments from these two proteins, containing the first alpha-helix of a colicinlike hydrophobic hairpin (alpha-helix 5 of Bax and alpha-helix 6 of Bid). Both peptides readily bind to synthetic lipid vesicles, where they adopt predominantly alpha-helical structures and induce the release of entrapped calcein. In planar lipid membranes they fo…

Models MolecularMolecular Sequence DataBiophysicsApoptosisPeptideIn Vitro TechniquesBiophysical PhenomenaIon ChannelsPermeabilityProtein Structure Secondarychemistry.chemical_compoundBcl-2-associated X proteinSpectroscopy Fourier Transform InfraredHumansChannels Receptors and Electrical SignalingAmino Acid SequencePeptide sequenceIon channelbcl-2-Associated X Proteinchemistry.chemical_classificationbiologyChemistryCircular DichroismPeptide FragmentsCell biologyCalceinMembraneProto-Oncogene Proteins c-bcl-2CytoplasmMultiprotein ComplexesLiposomesbiology.proteinPèptidsCarrier ProteinsBacterial outer membraneProteïnesBH3 Interacting Domain Death Agonist ProteinBiophysical Journal
researchProduct

Structural characterization of the Borrelia burgdorferi outer surface protein BBA73 implicates dimerization as a functional mechanism.

2013

Borrelia burgdorferi, which is the causative agent of Lyme disease, is transmitted from infected Ixodes ticks to a mammalian host following a tick bite. Upon changing the host organism from an Ixodes tick to a warm-blooded mammal, the spirochete must adapt to very different conditions, which is achieved by altering the expression of several genes in response to a changing environment. Recently, considerable attention has been devoted to several outer surface proteins, including BBA73, that undergo dramatic upregulation during the transmission of B. burgdorferi from infected Ixodes ticks to mammals and that are thought to be important for the establishment and maintenance of the infection. T…

Models MolecularMolecular Sequence DataStatic ElectricityBiophysicsCrystallography X-RayBiochemistryProtein Structure SecondaryMicrobiologyProtein structureAnimalsAmino Acid SequenceBorrelia burgdorferiCloning MolecularProtein Structure QuaternaryMolecular BiologyPeptide sequenceLyme DiseaseBinding SitesbiologyIxodesSequence Homology Amino AcidCell BiologyProtein superfamilyLigand (biochemistry)biology.organism_classificationSolutionsMembrane proteinBorrelia burgdorferiLyme disease microbiologyIxodesProtein MultimerizationBacterial Outer Membrane ProteinsBiochemical and biophysical research communications
researchProduct