Search results for "Structural Biology."

showing 10 items of 822 documents

Mass Spectrometry and Structural Biology Techniques in the Studies on the Coronavirus-Receptor Interaction

2020

Mass spectrometry and some other biophysical methods, have made substantial contributions to the studies on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and human proteins interactions. The most interesting feature of SARS-CoV-2 seems to be the structure of its spike (S) protein and its interaction with the human cell receptor. Mass spectrometry of spike S protein revealed how the glycoforms are distributed across the S protein surface. X-ray crystallography and cryo-electron microscopy made huge impact on the studies on the S protein and ACE2 receptor protein interaction, by elucidating the three-dimensional structures of these proteins and their conformational changes. The…

Models MolecularProtein Conformation alpha-HelicalvirusesGene ExpressionPharmaceutical ScienceReviewPlasma protein bindingSevere Acute Respiratory Syndromemedicine.disease_causeAnalytical Chemistry0302 clinical medicineDrug Discovery030212 general & internal medicineReceptorPeptide sequenceCoronavirus0303 health sciencesChemistrySevere acute respiratory syndrome-related coronavirusBiochemistryChemistry (miscellaneous)Host-Pathogen InteractionsSpike Glycoprotein CoronavirusReceptors VirusMolecular MedicineAngiotensin-Converting Enzyme 2Coronavirus InfectionsProtein BindingglycosylationSARS coronavirusPneumonia Viralstructural techniquesSequence alignmentPeptidyl-Dipeptidase AMass spectrometrylcsh:QD241-441Betacoronavirus03 medical and health scienceslcsh:Organic chemistryspike protein-ACE2 interactionmedicineHumansProtein Interaction Domains and MotifsAmino Acid SequencePhysical and Theoretical ChemistryBinding sitePandemics030304 developmental biologyBinding SitesSARS-CoV-2Organic ChemistryCOVID-19MSStructural biologyProtein Conformation beta-StrandSequence AlignmentMolecules
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Crystal structures of bR(D85S) favor a model of bacteriorhodopsin as a hydroxyl-ion pump

2003

AbstractStructural features on the extracellular side of the D85S mutant of bacteriorhodopsin (bR) suggest that wild-type bR could be a hydroxyl-ion pump. A position between the protonated Schiff base and residue 85 serves as an anion-binding site in the mutant protein, and hydroxyl ions should have access to this site during the O-intermediate of the wild-type bR photocycle. The guanidinium group of R82 is proposed (1) to serve as a shuttle that eliminates the Born energy penalty for entry of an anion into this binding pocket, and conversely, (2) to block the exit of a proton or a related proton carrier.

Models MolecularProtein ConformationAnion Transport ProteinsBiophysicsBacteriorhodopsinProtonationCrystal structureCrystallography X-RayBiochemistryIon pumpIonchemistry.chemical_compoundResidue (chemistry)Structural BiologyMutant proteinHydroxidesGeneticsMolecular BiologyIon TransportSchiff basebiologyChemistryBacteriorhodopsinCell BiologyCrystallographyIon pumpBacteriorhodopsinsMutationbiology.proteinHydroxyl ionProtonsFEBS Letters
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Membrane insertion and topology of the TRanslocating chain-Associating Membrane protein (TRAM)

2011

The translocating chain-associating membrane protein (TRAM) is a glycoprotein involved in the translocation of secreted proteins into the endoplasmic reticulum (ER) lumen and in the insertion of integral membrane proteins into the lipid bilayer. As a major step toward elucidating the structure of the functional ER translocation/insertion machinery, we have characterized the membrane integration mechanism and the transmembrane topology of TRAM using two approaches: photocross-linking and truncated C-terminal reporter tag fusions. Our data indicate that TRAM is recognized by the signal recognition particle and translocon components, and suggest a membrane topology with eight transmembrane seg…

Models MolecularProtein ConformationEndoplasmic ReticulumModels BiologicalProtein Structure SecondaryMiceMembranes (Biologia)Structural BiologyAnimalsMolecular BiologyIntegral membrane proteinSignal recognition particleMembrane GlycoproteinsbiologyMembrane transport proteinPeripheral membrane proteinProteïnes de membranaIntracellular MembranesTransloconTransmembrane proteinProtein Structure TertiaryMembrane proteinBiochemistryMembrane topologybiology.proteinBiophysics
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Self-assembling of poly(aspartic acid) with bovine serum albumin in aqueous solutions

2016

Abstract Macromolecular co-assemblies built up in aqueous solutions, by using a linear polypeptide, poly(aspartic acid) (PAS), and a globular protein, bovine serum albumin (BSA), have been studied. The main interest was to identify the optimum conditions for an interpenetrated complex formation in order to design materials suitable for biomedical applications, such as drug delivery systems. BSA surface possesses several amino- and carboxylic groups available for covalent modification, and/or bioactive substances attachment. In the present study, mixtures between PAS and BSA were investigated at 37 °C in dilute aqueous solution by viscometry, dynamic light scattering and zeta potential deter…

Models MolecularProtein ConformationGlobular protein02 engineering and technology010402 general chemistry01 natural sciencesBiochemistryDynamic light scatteringStructural BiologyAspartic acidZeta potentialAnimalsBovine serum albuminMolecular Biologychemistry.chemical_classificationAqueous solutionChromatographybiologyChemistryWaterSerum Albumin BovineGeneral MedicineHydrogen-Ion Concentration021001 nanoscience & nanotechnology0104 chemical sciencesSolutionsDrug deliverybiology.proteinCattlePeptides0210 nano-technologyProtein BindingNuclear chemistryMacromoleculeInternational Journal of Biological Macromolecules
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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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Structure of Aspergillus niger epoxide hydrolase at 1.8 A resolution: implications for the structure and function of the mammalian microsomal class o…

2000

AbstractBackground: Epoxide hydrolases have important roles in the defense of cells against potentially harmful epoxides. Conversion of epoxides into less toxic and more easily excreted diols is a universally successful strategy. A number of microorganisms employ the same chemistry to process epoxides for use as carbon sources.Results: The X-ray structure of the epoxide hydrolase from Aspergillus niger was determined at 3.5 Å resolution using the multiwavelength anomalous dispersion (MAD) method, and then refined at 1.8 Å resolution. There is a dimer consisting of two 44 kDa subunits in the asymmetric unit. Each subunit consists of an α/β hydrolase fold, and a primarily helical lid over the…

Models MolecularProtein ConformationStereochemistryEpoxide10050 Institute of Pharmacology and Toxicology610 Medicine & healthEpoxide hydrolasechemistry.chemical_compoundProtein structure1315 Structural BiologyStructural BiologyMicrosomesHydrolase1312 Molecular BiologyAnimalsHumansBinding siteEpoxide hydrolaseMolecular BiologyX-ray crystallographyEpoxide HydrolasesMicrosomal epoxide hydrolasesDrug metabolismBinding SitesbiologyMADChemistryAspergillus nigerbiology.organism_classificationBiochemistryEpoxide HydrolasesMicrosome570 Life sciences; biologyAspergillus nigerDimerization
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Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism

2000

The enzymes tyrosinase, catecholoxidase and hemocyanin all share similar active sites, although their physiological functions differ. Hemocyanins serve as oxygen carrier proteins, and tyrosinases and catecholoxidases (commonly referred to as phenoloxidases in arthropods) catalyze the hydroxylation of monophenols or the oxidation of o-diphenols to o-quinones, or both. Tyrosinases are activated in vivo by limited proteolytic cleavage, which might open up substrate access to the catalytic site. It has recently been demonstrated that if hemocyanins are subjected to similar proteolytic treatments (in vitro) they also exhibit at least catecholoxidase reactivity. On the basis of their molecular st…

Models MolecularProtein ConformationTyrosinasemedicine.medical_treatmentchemical and pharmacologic phenomenaBiochemistrySubstrate SpecificityHydroxylationchemistry.chemical_compoundProtein structuremedicineAnimalsBinding siteCatechol oxidaseMolecular Biologychemistry.chemical_classificationBinding SitesMolecular StructurebiologyMonophenol MonooxygenaseHemocyaninEnzyme ActivationEnzymechemistryBiochemistryStructural biologyHemocyaninsbiology.proteinCatechol OxidaseTrends in Biochemical Sciences
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Bacteriophage P23-77 capsid protein structures reveal the archetype of an ancient branch from a major virus lineage.

2013

Summary It has proved difficult to classify viruses unless they are closely related since their rapid evolution hinders detection of remote evolutionary relationships in their genetic sequences. However, structure varies more slowly than sequence, allowing deeper evolutionary relationships to be detected. Bacteriophage P23-77 is an example of a newly identified viral lineage, with members inhabiting extreme environments. We have solved multiple crystal structures of the major capsid proteins VP16 and VP17 of bacteriophage P23-77. They fit the 14 Å resolution cryo-electron microscopy reconstruction of the entire virus exquisitely well, allowing us to propose a model for both the capsid archi…

Models MolecularProtein ConformationViral proteinLineage (evolution)virusesCrystallography X-Raymedicine.disease_causeArticleVirusViral AssemblyBacteriophage03 medical and health sciencesProtein structureStructural BiologymedicineBacteriophagesMolecular Biology030304 developmental biologySequence (medicine)0303 health sciencesbiology030306 microbiologyCryoelectron Microscopyta1183ta1182biology.organism_classificationVirology3. Good healthCapsidEvolutionary biologyCapsid ProteinsCrystallizationStructure (London, England : 1993)
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Assessing model accuracy using the homology modeling automatically software

2007

Homology modeling is a powerful technique that greatly increases the value of experimental structure determination by using the structural information of one protein to predict the structures of homologous proteins. We have previously described a method of homology modeling by satisfaction of spatial restraints (Li et al., Protein Sci 1997;6:956-970). The Homology Modeling Automatically (HOMA) web site,http://www-nmr.cabm.rutgers.edu/HOMA, is a new tool, using this method to predict 3D structure of a target protein based on the sequence alignment of the target protein to a template protein and the structure coordinates of the template. The user is presented with the resulting models, togeth…

Models MolecularProtein Conformationbusiness.industryProteinsSequence alignmentStructure validationComputational biologyProtein superfamilyMachine learningcomputer.software_genreBiochemistryHomology (biology)Structural genomicsProtein structureStructural BiologyArtificial intelligenceTarget proteinHomology modelingbusinessMolecular BiologycomputerSoftwareMathematicsProteins: Structure, Function, and Bioinformatics
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Cis autocatalytic cleavage of glycine-linked Zika virus NS2B-NS3 protease constructs.

2019

The flaviviral heterodimeric serine protease NS2B-NS3, consisting of the NS3 protease domain and the NS2B co-factor, is essential for ZIKA virus maturation and replication in cells. For in vitro studies a 'linked' construct, where a polyglycine linker connects NS2BCF and NS3pro , is often used. This construct undergoes autocatalytic cleavage. Here, we show that linked ZIKV NS2BCF -NS3pro is cleaved in cis in the NS2BCF exclusively at position R95 and not at the previously proposed alternate cleavage site at residue R29 in the NS3pro . Cleavage neither affects protease stability nor activity, despite some observed differences in spectroscopic behavior. This minimally modified construct may t…

Models MolecularProtein Conformationmedicine.medical_treatmentBiophysicsViral Nonstructural ProteinsCleavage (embryo)ArginineVirus ReplicationBiochemistryCatalysisZika virus03 medical and health sciencesViral ProteinsStructural BiologyGeneticsmedicineHomeostasisMolecular Biology030304 developmental biologySerine protease0303 health sciencesNS3ProteasebiologyChemistryCircular Dichroism030302 biochemistry & molecular biologySerine EndopeptidasesCell BiologyZika Virusbiology.organism_classificationIn vitroRecombinant ProteinsFlavivirusSpectrometry FluorescenceBiochemistrybiology.proteinProtein MultimerizationPeptidesLinkerPeptide HydrolasesFEBS lettersReferences
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