Search results for "Dimer"

showing 10 items of 558 documents

Influence of the C-terminus of the glycophorin A transmembrane fragment on the dimerization process

2000

The monomer-dimer equilibrium of the glycophorin A (GpA) transmembrane (TM) fragment has been used as a model system to investigate the amino acid sequence requirements that permit an appropriate helix-helix packing in a membrane‐mimetic environment. In particular, we have focused on a region of the helix where no crucial residues for packing have been yet reported. Various deletion and replacement mutants in the C‐terminal region of the TM fragment showed that the distance between the dimerization motif and the flanking charged residues from the cytoplasmic side of the protein is important for helix packing. Furthermore, selected GpA mutants have been used to illustrate the rearrangement o…

Models MolecularStereochemistryProtein ConformationMutantMolecular Sequence DataBiochemistryProtein structureGlycophorinAmino Acid SequenceGlycophorinsMolecular BiologyProtein secondary structurePeptide sequencebiologyChemistryC-terminusProteïnes de membranaMembrane ProteinsTransmembrane proteinPeptide FragmentsBiochemistryMembrane proteinbiology.proteinDimerizationResearch Article
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Structure of a molluscan hemocyanin didecamer (HtH1 from Haliotis tuberculata) at 12 Å resolution by cryoelectron microscopy

2000

A 12 A resolution three-dimensional density map of the Haliotis tuberculata hemocyanin type 1 (HtH1) didecamer has been obtained by cryoelectron microscopy of unstained molecules and angular reconstitution. The dyad symmetry of the 8 MDa D5 HtH1 didecamer, formed by the pairing of two asymmetric 4 MDa ring-like C5 decamers, is emphasised. The major and minor surface helical grooves of the didecamer are well defined, in agreement with earlier data on molluscan hemocyanins. The location of the obliquely orientated repeating unit, a subunit dimer, within the decamer has been defined. Following interactive extraction of this dimer, several new structural features of the dimer and of the subunit…

Models MolecularSteric effectsDimermedicine.medical_treatmentProtein subunitCryoelectron MicroscopyHemocyaninBiologyCleavage (embryo)chemistry.chemical_compoundCrystallographychemistryMolluscaStructural BiologyHemocyaninsMicroscopyImage Processing Computer-AssistedmedicineAnimalsMoleculeProtein Structure QuaternaryDimerizationMolecular BiologyDyad symmetryJournal of Molecular Biology
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Self-Sorting Dimerization of Tetraurea Calix[4]arenes

2007

Calix[4]arenes substituted by four urea functions are self-complementary molecules that spontaneously combine in apolar solvents in the presence of an ammonium salt to form dimeric capsules held together by a belt of hydrogen bonds. In the presence of tetraethylammonium salts, the Et4N+ cation is included as a guest. The sorting between dimeric capsules formed in a mixture of calix[4]arenes directly depends on the steric crowding of the substituents grafted on the urea groups whether aromatic derivatives or aliphatic chains linking urea functions in mono-, di-, or tetraloop structures. Simple rules allow one to anticipate which capsules will be exclusively formed when calix[4]arenes are mix…

Models MolecularSteric effectsMagnetic Resonance SpectroscopyMolecular StructureHydrogen bondStereochemistryDimerOrganic ChemistryStereoisomerismNuclear magnetic resonance spectroscopyInclusion compoundchemistry.chemical_compoundPhenolschemistryPolymer chemistryCalixareneUreaMoleculeCalixarenesAliphatic compoundDimerizationThe Journal of Organic Chemistry
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Reasons for the exclusive formation of heterodimeric capsules between tetra-tolyl and tetra-tosylurea calix[4]arenes

2007

The selective heterodimerization of tetra-tolyl (1a) and tetra-tosylurea (1b) calixarenes, serendipitously found by Rebek et al. (R. K. Castellano, B. H. Kim and J. Rebek, Jr., J. Am. Chem. Soc., 1997, 119, 12671–12672), has been used for the construction of highly sophisticated macrocycles and well-defined supramolecular assemblies. Regrettably, hitherto, neither the exact structure of these heterodimers nor the reason for their exclusive formation is known. We present molecular dynamics simulations using the AMBER force field in explicit chloroform solvent for the two homodimers, the heterodimer and the two uncomplexed tetra-urea calixarenes. The rigid rotation about the C–S–N–C bond of t…

Models MolecularSteric effectsMagnetic Resonance SpectroscopyMolecular StructurebiologyChemistryHydrogen bondStereochemistryOrganic ChemistrySupramolecular chemistryCapsulesHydrogen Bondingbiology.organism_classificationBiochemistrySolutionsTosyl CompoundsSolventMolecular dynamicsCalixareneProton NMRUreaTetraCalixarenesPhysical and Theoretical ChemistryDimerizationOrganic & Biomolecular Chemistry
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Molecules with New Topologies Derived from Hydrogen-Bonded Dimers of Tetraurea Calix[4]arenes

2008

Tetraurea calix[4]arenes 2 have been synthesized in which two adjacent aryl urea residues are connected to a loop by an aliphatic chain -O-(CH(2))(n)-O-. The remaining urea residues have a bulky 3,5-di-tert-butylphenyl residue and an omega-alkenyloxyphenyl residue. Since this bulky residue cannot pass through the loop, only one homodimer (22) is formed in apolar solvents, for steric reasons, in which the two alkenyl residues penetrate the two macrocyclic loops. Covalent connection of these alkenyl groups by olefin metathesis followed by hydrogenation creates compounds 3, which consist of molecules with hitherto unknown topology. Their molecular structure was confirmed by (1)H NMR spectrosco…

Models MolecularSteric effectsSpectrometry Mass Electrospray IonizationMagnetic Resonance SpectroscopyStereochemistryArylOrganic ChemistryHydrogen BondingGeneral ChemistryCatalysischemistry.chemical_compoundResidue (chemistry)PhenolschemistryCovalent bondCalixareneUreaProton NMRMoleculeCalixarenesDimerizationChemistry - A European Journal
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Energy transfers in monomers, dimers, and trimers of zinc(II) and palladium(II) porphyrins bridged by rigid Pt-containing conjugated organometallic s…

2009

A series of linear monomers (spacer-M(P)), dimers (M(P)-spacer-M'(P)), and trimers (M(P)-spacer-M'(P)-spacer-M(P)) of spacer/metalloporphyrin systems (M' = Zn, M = Zn, Pd, P = porphyrin, and spacer = trans-C(6)H(4)C[triple bond]CPtL(2)C[triple bond]CC(6)H(4)- (L = PEt(3))) including mixed metalloporphyrin compounds, were synthesized and characterized. The S(1) and T(1) energy transfers Pd(P)*--Zn(P) occur with rates of approximately 2 x 10(9) s(-1), S(1), and 0.15 x 10(3) (slow component) and 4.3 x 10(3) s(-1) (fast component), T(1). On the basis of a literature comparison with a related dyad, the Pt atom in the conjugated chain slows down the transfers. The excitation in the absorption ban…

Models MolecularTime FactorsOrganoplatinum CompoundsStereochemistryMetalloporphyrinsMolecular Conformationchemistry.chemical_elementZincConjugated system010402 general chemistryLigands01 natural sciences7. Clean energyAbsorptionInorganic Chemistrychemistry.chemical_compoundAtomtrimerPhysical and Theoretical ChemistryComputingMilieux_MISCELLANEOUSmetalloporphyrinenergy transfer010405 organic chemistrySpectrum AnalysiszincmonomerdimerpalladiumPorphyrin0104 chemical sciences3. Good health[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryCrystallographyMonomerchemistryAbsorption bandLuminescent Measurements[ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistryconjugated organometallic spacerDimerizationExcitationPalladium
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Theoretical insight into the intrinsic ultrafast formation of cyclobutane pyrimidine dimers in UV-irradiated DNA: thymine versus cytosine.

2008

The higher formation yields measured in the ultrafast photoinduced formation of cyclobutane thymine dimers (T T) with respect to those of cytosine (C C) are explained, on the basis of ab initio CASPT2 results, by the existence in thymine of more reactive orientations and a less efficient photoreversibility, whereas in cytosine the funnel toward the photolesion becomes competitive with that mediating the internal conversion of the excited-cytosine monomer.

Models MolecularTime FactorsUltraviolet RaysAb initioPyrimidine dimerDNAInternal conversion (chemistry)PhotochemistrySurfaces Coatings and FilmsThymineCyclobutanechemistry.chemical_compoundCytosineMonomerchemistryPyrimidine DimersMaterials ChemistryNucleic Acid ConformationPhysical and Theoretical ChemistryCytosineDNAThymineDNA DamageThe journal of physical chemistry. B
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Structure of the human filamin A actin-binding domain.

2009

Filamin A (FLNa) is a large dimeric protein that binds to actin filaments via its actin-binding domain (ABD). The crystal structure of this domain was solved at 3.2 A resolution. The domain adopts a closed conformation typical of other ABDs, but also forms a dimer both in crystallization conditions and in solution. The structure shows the localization of the residues mutated in patients with periventricular nodular heterotopia or otopalatodigital syndrome. Structural analysis predicts that mutations in both types of disorder may affect actin binding.

Models Molecularanimal structuresDimerFilaminsmacromolecular substancesFilaminCalponin homology domainCrystallography X-Raychemistry.chemical_compoundContractile ProteinsStructural BiologyFLNAHumansProtein Interaction Domains and MotifsActin-binding proteinProtein Structure QuaternaryActinbiologyMicrofilament ProteinsGeneral MedicineActinschemistryStructural Homology ProteinDomain (ring theory)Mutationbiology.proteinBiophysicsBinding domainProtein BindingActa crystallographica. Section D, Biological crystallography
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The C-terminal rod 2 fragment of filamin A forms a compact structure that can be extended

2012

Filamins are large proteins that cross-link actin filaments and connect to other cellular components. The C-terminal rod 2 region of FLNa (filamin A) mediates dimerization and interacts with several transmembrane receptors and intracellular signalling adaptors. SAXS (small-angle X-ray scattering) experiments were used to make a model of a six immunoglobulin-like domain fragment of the FLNa rod 2 (domains 16–21). This fragment had a surprising three-branched structural arrangement, where each branch was made of a tightly packed two-domain pair. Peptides derived from transmembrane receptors and intracellular signalling proteins induced a more open structure of the six domain fragment. Mutagen…

Models Moleculargenetics [Receptors Dopamine D3]metabolism [Recombinant Proteins]Protein Conformationgenetics [Antigens CD18]chemistry [Recombinant Proteins]Plasma protein bindingCrystallography X-RayLigandsFilaminmetabolism [Antigens CD18]metabolism [Cytoskeletal Proteins]BiochemistryfilaminsContractile ProteinsProtein structuremetabolism [Peptide Fragments]FLNAchemistry [Antigens CD18]genetics [Cell Adhesion Molecules]Small-angle X-ray scatteringMicrofilament Proteinsgenetics [Contractile Proteins]Recombinant Proteinschemistry [Receptors Dopamine D3]FBLIM1 protein humanddc:540Domain (ring theory)DimerizationProtein Bindingchemistry [Contractile Proteins]FilaminsAntigens CD18metabolism [Cell Adhesion Molecules]BiologyScattering Small Anglemetabolism [Receptors Dopamine D3]Humanschemistry [Microfilament Proteins]Protein Interaction Domains and Motifsmetabolism [Mutant Proteins]DRD3 protein humanMolecular Biologymetabolism [Contractile Proteins]Actingenetics [Cytoskeletal Proteins]Cryoelectron MicroscopyMutagenesista1182Receptors Dopamine D3metabolism [Microfilament Proteins]Cell Biologychemistry [Cell Adhesion Molecules]genetics [Peptide Fragments]Peptide FragmentsCytoskeletal ProteinsCrystallographychemistry [Mutant Proteins]chemistry [Peptide Fragments]CD18 AntigensBiophysicschemistry [Cytoskeletal Proteins]Mutant Proteinsgenetics [Microfilament Proteins]Cell Adhesion MoleculesBiochemical Journal
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Interactions of zinc octacarboxyphthalocyanine with selected amino acids and with albumin

2015

Effect of selected amino acids (glycine, l-histidine, l-cysteine, l-serine, l-tryptophan) and albumin on the spectroscopic properties and photostability of zinc octacarboxyphthalocyanine (ZnPcOC) was explored in the phosphate buffer at a pH of 7.0. The photodegradation of ZnPcOC alone and in the presence of amino acids or albumin has been investigated in aqueous phase using UV-366 nm and daylight irradiation. Kinetic analysis showed that the interaction with amino acids or albumin enhances the photostability of ZnPcOC. To answer the question of how zinc phthalocyanine interacts with amino acids extensive DFT calculations were performed. Analysis of the optimized geometry features of ZnPcOC:…

Models Molecularzinc octacarboxyphthalocyanineIndolesUltraviolet Rayschemistry.chemical_element02 engineering and technologyZincIsoindoles010402 general chemistryPhotochemistry01 natural sciencesAnalytical Chemistrychemistry.chemical_compoundPolymer chemistryOrganometallic CompoundsWater environmentAnimalsAmino AcidsPhotodegradationInstrumentationSpectroscopytheoretical calculationschemistry.chemical_classificationPhotolysisAqueous two-phase systemAlbuminSerum Albumin BovineUV–Vis spectra021001 nanoscience & nanotechnologyAtomic and Molecular Physics and Optics0104 chemical sciencesAmino acidphotodynamic therapychemistryZinc CompoundsGlycinePhthalocyanineCattleSpectrophotometry Ultravioletprotein0210 nano-technologyDimerizationamino acidSpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
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