Search results for " Crystal"

showing 10 items of 3073 documents

A community resource of experimental data for NMR / X-ray crystal structure pairs

2015

We have developed an online NMR / X-ray Structure Pair Data Repository. The NIGMS Protein Structure Initiative (PSI) has provided many valuable reagents, 3D structures, and technologies for structural biology. The Northeast Structural Genomics Consortium was one of several PSI centers. NESG used both X-ray crystallography and NMR spectroscopy for protein structure determination. A key goal of the PSI was to provide experimental structures for at least one representative of each of hundreds of targeted protein domain families. In some cases, structures for identical (or nearly identical) constructs were determined by both NMR and X-ray crystallography. NMR spectroscopy and X-ray diffraction …

0301 basic medicineChemistryNuclear magnetic resonance crystallographyNuclear magnetic resonance spectroscopyBiochemistryStructural genomics03 medical and health sciencesCrystallographyStructural bioinformatics030104 developmental biologyProtein structureStructural biologyTriple-resonance nuclear magnetic resonance spectroscopyMolecular BiologyProtein Structure InitiativeProtein Science
researchProduct

Proton Leakage Is Sensed by IM30 and Activates IM30-Triggered Membrane Fusion

2020

The inner membrane-associated protein of 30 kDa (IM30) is crucial for the development and maintenance of the thylakoid membrane system in chloroplasts and cyanobacteria. While its exact physiological function still is under debate, it has recently been suggested that IM30 has (at least) a dual function, and the protein is involved in stabilization of the thylakoid membrane as well as in Mg2+-dependent membrane fusion. IM30 binds to negatively charged membrane lipids, preferentially at stressed membrane regions where protons potentially leak out from the thylakoid lumen into the chloroplast stroma or the cyanobacterial cytoplasm, respectively. Here we show in vitro that IM30 membrane binding…

0301 basic medicineChloroplastsMembrane lipidsmembrane fusionMg2+CyanobacteriaThylakoidsCatalysisArticleVipp1Inorganic Chemistrylcsh:Chemistry03 medical and health sciencesMembrane Lipidsquartz crystal microbalanceProtein structureBacterial ProteinsPhysical and Theoretical ChemistryMg<sup>2+</sup>membrane bindingMolecular Biologylcsh:QH301-705.5SpectroscopyMembranes030102 biochemistry & molecular biologyChemistrypHOrganic ChemistrySynechocystisCD spectroscopyLipid bilayer fusionMembrane Proteinsfood and beveragesGeneral Medicinethylakoid membraneComputer Science ApplicationsChloroplastChloroplast stroma030104 developmental biologyMembranelcsh:Biology (General)lcsh:QD1-999CytoplasmThylakoidBiophysicsProtonsIM30Protein BindingInternational Journal of Molecular Sciences
researchProduct

Non-essential role for cilia in coordinating precise alignment of lens fibres

2016

The primary cilium, a microtubule-based organelle found in most cells, is a centre for mechano-sensing fluid movement and cellular signalling, notably through the Hedgehog pathway. We recently found that each lens fibre cell has an apically situated primary cilium that is polarised to the side of the cell facing the anterior pole of the lens. The direction of polarity is similar in neighbouring cells so that in the global view, lens fibres exhibit planar cell polarity (PCP) along the equatorial-anterior polar axis. Ciliogenesis has been associated with the establishment of PCP, although the exact relationship between PCP and the role of cilia is still controversial. To test the hypothesis t…

0301 basic medicineEmbryologyBBSomeBiologyArticle03 medical and health sciences0302 clinical medicineIntraflagellar transportMicrotubuleCiliogenesisLens CrystallineAnimalsBasal bodyLens placodeCiliaCells CulturedMice KnockoutTumor Suppressor ProteinsCiliumCell PolarityEpithelial CellsAnatomyCell biologyCytoskeletal Proteins030104 developmental biologyFiber cellMicrotubule-Associated Proteins030217 neurology & neurosurgeryDevelopmental BiologyMechanisms of Development
researchProduct

Objective Assessment of Nuclear and Cortical Cataracts through Scheimpflug Images: Agreement with the LOCS III Scale.

2016

Purpose To assess nuclear and cortical opacities through the objective analysis of Scheimpflug images, and to check the correlation with the Lens Opacity Classification System III (LOCS III). Methods Nuclear and cortical opacities were graded according to the LOCS III rules after pupil dilation. The maximum and average pixel intensity values along an elliptical mask within the lens nucleus were taken to analyse nuclear cataracts. A new metric based on the percentage of opaque pixels within a region of interest was used to analyse cortical cataracts. The percentage of opaque pixels was also calculated for half, third and quarter areas from the region of interest’s periphery. Results The maxi…

0301 basic medicineMaleScheimpflug principlelcsh:MedicineDiagnostic Techniques OphthalmologicalSeverity of Illness IndexMachine Learning0302 clinical medicineMedicine and Health Scienceslcsh:ScienceOptical PropertiesLens (Anatomy)PhysicsAged 80 and overMultidisciplinaryApplied MathematicsSimulation and ModelingOphthalmic ProceduresCataract SurgeryMiddle AgedOptical LensesOptical EquipmentPhysical SciencesEngineering and TechnologyFemaleAnatomyAlgorithmsResearch ArticleOpacityAdultDiagnostic Imagingmedicine.medical_specialtyComputer and Information SciencesScale (ratio)OpacityImaging TechniquesOcular AnatomyMaterials ScienceMaterial PropertiesEquipmentSurgical and Invasive Medical ProceduresImage AnalysisResearch and Analysis MethodsLens nucleusCataract03 medical and health sciencesMachine Learning AlgorithmsYoung AdultCataractsRegion of interestOcular SystemArtificial IntelligenceOphthalmologymedicineHumansAgedPixelCataractslcsh:RBiology and Life SciencesCorrectionLens Nucleus CrystallineLens Cortex Crystallinemedicine.diseaseIntensity (physics)Ophthalmology030104 developmental biologyLens DisordersCase-Control Studies030221 ophthalmology & optometryEyesCognitive Sciencelcsh:QHeadMathematicsNeurosciencePloS one
researchProduct

Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases

2020

13 páginas, 6 figuras, 3 tablas

0301 basic medicineModels MolecularBioquímicaHistidine KinaseProtein ConformationScience030106 microbiologyPhosphataseGeneral Physics and AstronomyMicrobiologiaCrystallography X-RayModels BiologicalBiochemistryMicrobiologyGeneral Biochemistry Genetics and Molecular BiologyCatalysisArticleEnzyme catalysis03 medical and health sciencesResidue (chemistry)Protein structureBacterial ProteinsMultienzyme ComplexesHistidineThermotoga maritimaPhosphorylationlcsh:ScienceAuthor CorrectionHistidineX-ray crystallographyMultidisciplinaryEffectorChemistryEscherichia coli ProteinsQGeneral ChemistryHydrogen-Ion ConcentrationResponse regulator030104 developmental biologyBiochemistryMutationTrans-ActivatorsPhosphorylationlcsh:QBacterial Outer Membrane Proteins
researchProduct

On the (un)coupling of the chromophore, tongue interactions, and overall conformation in a bacterial phytochrome

2018

Phytochromes are photoreceptors in plants, fungi, and various microorganisms and cycle between metastable red light-absorbing (Pr) and far-red light-absorbing (Pfr) states. Their light responses are thought to follow a conserved structural mechanism that is triggered by isomerization of the chromophore. Downstream structural changes involve refolding of the so-called tongue extension of the phytochrome-specific GAF-related (PHY) domain of the photoreceptor. The tongue is connected to the chromophore by conserved DIP and PRXSF motifs and a conserved tyrosine, but the role of these residues in signal transduction is not clear. Here, we examine the tongue interactions and their interplay with …

0301 basic medicineModels MolecularCrystallography X-RayBiochemistrybakteeritProtein structurephotoconversionchromophore-binding domainTransferasestructural biologyCRYSTAL-STRUCTURETyrosineDEINOCOCCUS-RADIODURANSbiologyPhytochromeChemistryREARRANGEMENTSProtein Structure and FoldingDeinococcusmutagenesisBinding domainSignal TransductionMODULEPLANT PHYTOCHROMEPhenylalaninefotobiologia03 medical and health sciencesBacterial Proteinsprotein conformationcell signalingprotein structureBACTERIOPHYTOCHROMEMolecular BiologyX-ray crystallographysoluviestintäphytochromeAGP1BINDING DOMAINBinding Sitesta114030102 biochemistry & molecular biologyta1182Deinococcus radioduransCell BiologyChromophorebiology.organism_classificationphotoreceptor030104 developmental biologyStructural biologyFTIRBiophysicsTyrosineproteiinit3111 Biomedicineröntgenkristallografia
researchProduct

2016

AbstractPhytochromes are a family of photoreceptors that control light responses of plants, fungi and bacteria. A sequence of structural changes, which is not yet fully understood, leads to activation of an output domain. Time-resolved serial femtosecond crystallography (SFX) can potentially shine light on these conformational changes. Here we report the room temperature crystal structure of the chromophore-binding domains of the Deinococcus radiodurans phytochrome at 2.1 Å resolution. The structure was obtained by serial femtosecond X-ray crystallography from microcrystals at an X-ray free electron laser. We find overall good agreement compared to a crystal structure at 1.35 Å resolution d…

0301 basic medicineMultidisciplinaryMaterials science030102 biochemistry & molecular biologyPhytochromeResolution (electron density)Crystal structureChromophoreSACLA03 medical and health sciencesCrystallography030104 developmental biologyProtein structureFemtosecondX-ray crystallographyScientific Reports
researchProduct

Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein

2016

Many biological processes depend on detecting and responding to light. The response is often mediated by a structural change in a protein that begins when absorption of a photon causes isomerization of a chromophore bound to the protein. Pande et al. used x-ray pulses emitted by a free electron laser source to conduct time-resolved serial femtosecond crystallography in the time range of 100 fs to 3 ms. This allowed for the real-time tracking of the trans-cis isomerization of the chromophore in photoactive yellow protein and the associated structural changes in the protein.Science, this issue p. 725A variety of organisms have evolved mechanisms to detect and respond to light, in which the re…

0301 basic medicinePhotoreceptorsTime FactorsPhotoisomerizationLightProtein ConformationPhotochemistryPhotoreceptors MicrobialMYOGLOBINProtein structureMicrobialX-RAY-DIFFRACTIONPHOTOISOMERIZATIONMOTIONSchromophoresta116MultidisciplinarySPECTROSCOPYCrystallographyChemistryPhotochemical ProcessesTime resolved crystallographyTIMEMultidisciplinary SciencesPicosecondFemtosecondphotoactive proteinsScience & Technology - Other Topicsddc:500IsomerizationStereochemistryGeneral Science & TechnologyConjugated systemArticle03 medical and health sciencesBacterial ProteinsIsomerismEXCITATIONx-ray crystallographyPhotonsScience & TechnologyPHOTOCYCLEta114CHROMOPHOREta1182PATHWAYSChromophore030104 developmental biologyfree-electron laserssense organstrans-cis isomerization
researchProduct

Mapping molecular binding by means of conformational dynamics measurements

2017

[EN] Protein-protein interactions are key in virtually all biological processes. The study of these interactions and the interfaces that mediate them play a key role in the understanding of biological function. In particular, the observation of protein¿protein interactions in their dynamic environment is technically difficult. Here two surface analysis techniques, dual polarization interferometry and quartz crystal microbalance with dissipation monitoring, were paired for real-time mapping of the conformational dynamics of protein¿ protein interactions. Our approach monitors this dynamics in real time and in situ, which is a great advancement within technological platforms for drug discover…

0301 basic medicinePhysicsDrug discoveryMechanism (biology)General Chemical EngineeringDynamics (mechanics)Molecular bindingGeneral ChemistryQuartz crystal microbalance03 medical and health sciences030104 developmental biologyDual-polarization interferometryQUIMICA ANALITICABiological systemRSC Advances
researchProduct

The C-terminal region of human plasma fetuin-B is dispensable for the raised-elephant-trunk mechanism of inhibition of astacin metallopeptidases

2019

© The Author(s) 2019.

0301 basic medicineProteasesProtein Conformationlcsh:MedicineAstacoideaCrystallography X-RayCleavage (embryo)Protein Structure SecondaryArticleMice03 medical and health sciencesScissile bondHydrolaseAnimalsHumansAmino Acid Sequencelcsh:ScienceProtein secondary structureX-ray crystallographyBinding SitesMultidisciplinary030102 biochemistry & molecular biologyChemistrylcsh:RMetalloendopeptidasesProteasesFetuinFetuin-BCell biologyZincFertility030104 developmental biologyProteolysisMetalloproteaseslcsh:QAstacinLinkerScientific Reports
researchProduct