Search results for "angle"

showing 10 items of 1921 documents

NMR Solution Structure of the Non-RGD Disintegrin Obtustatin

2003

The solution structure of obtustatin, a novel non-RGD disintegrin of 41 residues isolated from Vipera lebetina obtusa venom, and a potent and selective inhibitor of the adhesion of integrin alpha(1)beta(1) to collagen IV, has been determined by two-dimensional nuclear magnetic resonance. Almost the whole set of chemical shifts for 1H, 13C and 15N were assigned at natural abundance from 2D homonuclear and heteronuclear 500 MHz, 600 MHz and 800 MHz spectra at pH 3.0 recorded at 298 K and 303 K. Final structural constraints consisted of 302 non-redundant NOE (95 long-range, 60 medium, 91 sequential and 56 intra-residue), four disulfide bond distances, five chi1 dihedral angles and four hydroge…

Models MolecularProtein ConformationStereochemistryDisintegrinsMolecular Sequence DataStatic ElectricityViper VenomsDihedral angleCrystallography X-RayStructural BiologyDisintegrinAnimalsAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyProtein secondary structureConformational isomerismRGD motifMolecular StructureSequence Homology Amino AcidbiologyHydrogen bondChemistryCircular DichroismChemical shiftHydrogen BondingHydrogen-Ion ConcentrationSolutionsKineticsHeteronuclear moleculebiology.proteinOligopeptidesJournal of Molecular Biology
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The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin

2012

International audience; The acknowledged success of the Monod-Wyman-Changeux (MWC) allosteric model stems from its efficacy in accounting for the functional behavior of many complex proteins starting with hemoglobin (the paradigmatic case) and extending to channels and receptors. The kinetic aspects of the allosteric model, however, have been often neglected, with the exception of hemoglobin and a few other proteins where conformational relaxations can be triggered by a short and intense laser pulse, and monitored by time-resolved optical spectroscopy. Only recently the application of time-resolved wide-angle X-ray scattering (TR-WAXS), a direct structurally sensitive technique, unveiled th…

Models MolecularProtein ConformationcooperativityMESH: Catalytic DomainCooperativity01 natural sciencesMESH: Recombinant ProteinsHemoglobinsProtein structureMESH: Protein ConformationCatalytic Domainprotein structural dynamicsMESH: Allosteric Site0303 health sciencesMultidisciplinaryallosterybiologyMESH: KineticsChemistryBiological SciencesRecombinant Proteins[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsMESH: HemoglobinsAllosteric SiteMESH: Models MolecularAdultMESH: MutationStereochemistryKineticsAllosteric regulation010402 general chemistry03 medical and health sciencesprotein conformational changesflash photolysisallostery; cooperativity; flash photolysis; hemoglobin; protein conformational changes; protein structural dynamics; time-resolved wide angle x ray scattering; time-resolved x-ray scatteringHumans030304 developmental biologytime-resolved X-ray scattering; protein conformational changes; cooperativity; flash photolysisMESH: Humanstime-resolved X-ray scatteringWild typeActive sitetime-resolved wide angle x ray scatteringMESH: AdulthemoglobinSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical sciencesprotein conformational changeKineticsAllosteric enzymeMutationbiology.proteinHemoglobin
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Small-angle X-ray Scattering-based Three-dimensional Reconstruction of the Immunogen KLH1 Reveals Different Oxygen-dependent Conformations

2003

For decades the respiratory protein keyhole limpet hemocyanin (KLH1) from the marine gastropod Megathura crenulata has been used widely as a potent immunostimulant, useful hapten carrier, and valuable agent in the treatment of bladder carcinoma. Although much information on the immunological properties of KLH1 is available, biochemical and structural data are still incomplete. Small-angle x-ray scattering revealed the existence of two conformations, an oxy state being slightly more compact than the deoxy state. Based on small-angle scattering curves, a newly developed Monte Carlo algorithm delivered a surface representation of proteins. The massive changes of the surfaces of reconstructed d…

Models MolecularProtein Conformationmedicine.medical_treatmentMegathura crenulataCrystallography X-RayBiochemistryAllosteric RegulationmedicineAnimalsScattering RadiationMoleculeAntigensMolecular BiologybiologyScatteringSmall-angle X-ray scatteringHemocyaninCell Biologybiology.organism_classificationOxygenRespiratory proteinMicroscopy ElectronCrystallographyMolluscaHemocyaninsbiology.proteinHaptenKeyhole limpet hemocyaninJournal of Biological Chemistry
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Crystal Structure of Human Filamin C Domain 23 and Small Angle Scattering Model for Filamin C 23–24 Dimer

2007

Filamin C is a dimeric, actin-binding protein involved in organization of cortical cytoskeleton and of the sarcomere. We performed crystallographic, small-angle X-ray scattering and analytical ultracentrifugation experiments on the constructs containing carboxy-terminal domains of the protein (domains 23-24 and 19-21). The crystal structure of domain 23 of filamin C showed that the protein adopts the expected immunoglobulin (Ig)-like fold. Small-angle X-ray scattering experiments performed on filamin C tandem Ig-like domains 23 and 24 reveal a dimer that is formed by domain 24 and that domain 23 has little interactions with itself or with domain 24, while the analytical ultracentrifugation …

Models MolecularProtein FoldingFilaminsDimermacromolecular substancesCrystal structureCrystallography X-RayFilaminSarcomereAnalytical Ultracentrifugationchemistry.chemical_compoundContractile ProteinsNickelStructural BiologyScattering Small AngleHumansMolecular BiologyBinding SitesSmall-angle X-ray scatteringScatteringMicrofilament ProteinsProtein Structure TertiaryCrystallographychemistrySmall-angle scatteringDimerizationUltracentrifugationJournal of Molecular Biology
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Small-angle X-ray scattering reveals compact domain-domain interactions in the N-terminal region of filamin C

2014

Filamins are multi-domain, actin cross-linking, and scaffolding proteins. In addition to the actin cross-linking function, filamins have a role in mechanosensor signaling. The mechanosensor function is mediated by domain-domain interaction in the C-terminal region of filamins. Recently, we have shown that there is a three-domain interaction module in the Nterminal region of filamins, where the neighboring domains stabilize the structure of the middle domain and thereby regulate its interaction with ligands. In this study, we have used small-angle X-ray scattering as a tool to screen for potential domain-domain interactions in the N-terminal region. We found evidence of four domain-domain in…

Models MolecularScaffold proteinProtein StructureProtein ConformationFilaminslcsh:Medicinemacromolecular substancesBiologyFilaminBiochemistryProtein–protein interactionProtein structureX-Ray Diffractioncompact domain-domain interactionsScattering Small AngleMacromolecular Structure AnalysisProtein InteractionsCytoskeletonlcsh:ScienceMolecular BiologyActinMultidisciplinarySmall-angle X-ray scatteringlcsh:Rta1182Biology and Life SciencesProteinsComputational BiologyRecombinant ProteinsProtein Structure TertiaryCell biologyCytoskeletal Proteinssmall-angle X-ray scatteringDomain (ring theory)Biophysicslcsh:QGlobular ProteinsStructural ProteinsResearch Articlefilamin CPloS One
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Glutamate 270 plays an essential role in K+-activation and domain closure ofThermus thermophilusisopropylmalate dehydrogenase

2014

The mutant E270A of Thermus thermophilus 3-isopropylmalate dehydrogenase exhibits largely reduced (∼1%) catalytic activity and negligible activation by K(+) compared to the wild-type enzyme. A 3-4 kcal/mol increase in the activation energy of the catalysed reaction upon this mutation could also be predicted by QM/MM calculations. In the X-ray structure of the E270A mutant a water molecule was observed to take the place of K(+). SAXS and FRET experiments revealed the essential role of E270 in stabilisation of the active domain-closed conformation of the enzyme. In addition, E270 seems to position K(+) into close proximity of the nicotinamide ring of NAD(+) and the electron-withdrawing effect…

Models MolecularStereochemistry030303 biophysicsMutantBiophysicsGlutamic AcidLarge scale facilities for research with photons neutrons and ionsSmall angle X-ray scatteringDehydrogenaseBiochemistry3-Isopropylmalate Dehydrogenase03 medical and health scienceschemistry.chemical_compoundIsopropylmalate dehydrogenaseFluorescence resonance energy transferStructural BiologyOxidoreductaseGeneticsMolecular BiologyX-ray crystallography030304 developmental biologychemistry.chemical_classificationSite-directed mutagenesis0303 health sciencesNicotinamidebiologyThermus thermophilusActivation by K+Cell BiologyThermus thermophilusbiology.organism_classificationProtein Structure TertiaryMOPSEnzyme ActivationKineticsCrystallographyEnzymechemistryMutationNAD+ kinaseFEBS Letters
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Solvent effects on the conformational preferences of model peptoids. MP2 study.

2014

The influence of aqueous environment on the main-chain conformation (ω0, ϕ, and ψ dihedral angles) of two model peptoids: N-acetyl-N-methylglycine N’-methylamide (Ac-N(Me)-Gly-NHMe) (1) and N-acetyl-N-methylglycine N’,N’-dimethylamide (Ac-N(Me)-Gly-NMe2) (2) was investigated by MP2/6-311++G(d,p) method. The Ramachandran maps of both studied molecules with cis and trans configuration of the N-terminal amide bond in the gas phase and in water environment were obtained and all energy minima localized. The polarizable continuum model was applied to estimate the solvation effect on conformation. Energy minima of the Ac-N(Me)-Gly-NHMe and Ac-N(Me)-Gly-NMe2 have been analyzed in terms of the possi…

Models MolecularStereochemistryMolecular ConformationDihedral angleBiochemistryPolarizable continuum modelPeptoidsStructural BiologyDrug DiscoveryWater environmentMolecular BiologyPharmacologysolvent effectMP2ChemistryHydrogen bondOrganic Chemistryconformational analysiscis - trans isomerisationSolvationHydrogen BondingGeneral MedicineN-methylationCrystallographyPCMSolventsMolecular MedicineSolvent effectsCis–trans isomerismRamachandran plotJournal of peptide science : an official publication of the European Peptide Society
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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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Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase

2017

Sensor histidine kinases are central to sensing in bacteria and in plants. They usually contain sensor, linker, and kinase modules and the structure of many of these components is known. However, it is unclear how the kinase module is structurally regulated. Here, we use nano- to millisecond time-resolved X-ray scattering to visualize the solution structural changes that occur when the light-sensitive model histidine kinase YF1 is activated by blue light. We find that the coiled coil linker and the attached histidine kinase domains undergo a left handed rotation within microseconds. In a much slower second step, the kinase domains rearrange internally. This structural mechanism presents a t…

Models MolecularkinaasitentsyymitHistidine KinaseLightProtein ConformationScienceQCrystallography X-RayArticleProtein Structure SecondaryaktivointiBacterial ProteinsProtein DomainsX-Ray DiffractionphotoactivationScattering Small AngleNanotechnologysensor histidine kinasesNature Communications
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Nonsurgical treatment of skeletal anterior open bite in adult patients: Posterior build-ups.

2016

ABSTRACT Objective: To (1) evaluate the efficacy of build-ups in the correction of anterior open bite in adults, (2) evaluate their efficacy in producing molar intrusion, (3) analyze skeletal and dental changes, and (4) assess the long-term stability. Materials and Methods: The sample consisted of 93 lateral cephalograms from 31 patients with skeletal and dental anterior open bite. The patients had received orthodontic treatment consisting of bonded resin blocks on the maxillary molars combined with Tip-Edge Plus bracket appliances. Cephalometric measurements were performed on radiographs taken before treatment (T1), after treatment (T2), and after a retention period (T3), which were analyz…

MolarAdultMaleTooth Movement TechniquesCephalometryOrthodontic BracketsRadiographyDentistryOrthodonticsMandibleOverbiteMalocclusion Angle Class II03 medical and health sciences0302 clinical medicineIncisorstomatognathic systemMaxillaOrthodontic Anchorage ProceduresMedicineHumansOrthodontic Appliance DesignOrthodonticsbusiness.industryMandibleOpen Bite030206 dentistryOriginal ArticlesCraniometryMolarOrthodontic Anchorage ProceduresIncisormedicine.anatomical_structureTreatment OutcomeMaxillaFemalebusiness030217 neurology & neurosurgeryThe Angle orthodontist
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