Search results for "conformational change"

showing 10 items of 69 documents

The Binding Mechanism of Epolactaene to Hsp60 Unveiled by in Silico Modelling

2016

Molecular Dynamics (MD) simulations and DFT/MM calculations were performed in order to rationalize available experimental results and to provide structural details on the binding mechanism of Epolactaene (EPO) to the 60 KDa Heat Shock Protein (Hsp60). The available crystal structure of Hsp60 represents the last step of the chaperone folding cycle, while the Hsp60-EPO complex was obtained by using a homology model of Hsp60, in order to simulate a state related to the beginning of the folding cycle (Rs1). The results of MD simulations point out that EPO shows the highest binding affinity for the empty ATP binding site. The presence of ATP opens a channel that allows the entrance of both EPO d…

0301 basic medicineConformational changeanimal structuresStereochemistryProteins · Molecular Dynamics · Density Functional Theory · Heat Shock Proteins · Epolactaene010402 general chemistry01 natural sciences03 medical and health sciencesMolecular dynamicschemistry.chemical_compoundHeat shock proteinHomology modelingBinding siteEpolactaenebiologyChemistrySettore BIO/16 - Anatomia UmanafungiGeneral ChemistrySettore CHIM/06 - Chimica Organica0104 chemical sciencesCrystallography030104 developmental biologyCovalent bondSettore CHIM/03 - Chimica Generale E InorganicaChaperone (protein)biology.protein
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Structural analysis of Cu(II) ligation to the 5'-GMP nucleotide by pulse EPR spectroscopy.

2007

JBIC Journal of Biological Inorganic Chemistry, 12 (6)

10120 Department of ChemistryConformational change1303 BiochemistryAnalytical chemistryGuanosine MonophosphateLigandsBiochemistrylaw.inventionInorganic Chemistrycopper; electron-nuclear double resonance; hyperfine sublevel correlation spectroscopy; pulse electron paramagnetic resonance spectroscopy; nucleotidelaw540 ChemistryOrganometallic CompoundsDNA Z-FormElectron paramagnetic resonanceHyperfine structurehyperfine sublevel correlation spectroscopyElectron nuclear double resonanceMolecular StructurePulsed EPRChemistryLigand1604 Inorganic ChemistryElectron Spin Resonance SpectroscopyDNAnucleotideSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)CrystallographyUnpaired electronpulse electron paramagnetic resonance spectroscopyNucleic Acid Conformationelectron-nuclear double resonanceTwo-dimensional nuclear magnetic resonance spectroscopyCopperJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
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Thermal induced conformational changes involved in the aggregation of beta-lactoglobulin

2005

Aggregation of proteins appears to be associated most often with conformational and structural changes that lead to exposure of some apolar residues. Depending on the native structure of the protein in exam, aggregation is a process that involves different mechanisms, whose time of occurrence and interplay can depend upon temperature. To single out information about the multistages of the aggregation pathway, here we investigate the thermally induced conformational and structural changes of the beta-lactoglobulin (BLG). The experimental approach consists in studying steady-state fluorescence spectra of intrinsic chromophores, two tryptophans, and Anylino-Naphthalene-Sulfonate dye (ANS) mole…

ANS emissionBeta-lactoglobulinProtein aggregationRayleigh scatteringCircular dichroismConformational changeFluorescence
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Thermodynamic versus Conformational Metastability in Fibril-Forming Lysozyme Solutions

2012

The role of intermolecular interaction in fibril-forming protein solutions and its relation with molecular conformation is a crucial aspect for the control and inhibition of amyloid structures. Here, we study the fibril formation and the protein-protein interactions of lysozyme at acidic pH and low ionic strength. The amyloid formation occurs after a long lag time and is preceded by the formation of oligomers, which seems to be off-pathway with respect to fibrillation. By measuring the osmotic isothermal compressibility and the collective diffusion coefficient of lysozyme in solution, we observe that the monomeric solution is kept in a thermodynamically metastable state by strong electrosta…

AmyloidConformational changeProtein ConformationDiffusionOsmolar ConcentrationHydrogen-Ion ConcentrationFibrilProtein tertiary structurePolyelectrolyteSurfaces Coatings and FilmsSolutionschemistry.chemical_compoundMonomerchemistryChemical physicsMetastabilityMaterials ChemistryThermodynamicsMuramidasePhysical and Theoretical ChemistryLysozymeProtein BindingThe Journal of Physical Chemistry B
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Redox-active crown ethers derived from biphenyl. Electrochemical and spectroscopic study of binding processes with alkali, alkali-earth and mercury s…

1998

Abstract Three new electroactive ligands, 3a, 3b and 3c, that contain the biphenyl frameworks in their structure were prepared. These new ligands presented three interesting characteristics: 1) they exhibited a reversible oxidation, 2) the oxidation induced a conformational change in the crown moiety and 3) they had two different coordination centers, the crown ether and the dimethylamino groups. Electrochemical and spectroscopic studies using alkali, alkali-earth and mercury salts were carried out.

Biphenylchemistry.chemical_classificationConformational changeAlkaline earth metalChemistryOrganic ChemistryInorganic chemistrychemistry.chemical_elementAlkali metalElectrochemistryBiochemistryMercury (element)chemistry.chemical_compoundDrug DiscoveryMoietyCrown etherTetrahedron
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Biphenyl macrolactams in anion complexation. Selective naked-eye fluoride recognition

2004

Two colorimetric anion sensors 1 and 2 allow for the selective differentiation of fluoride in the presence of other anions. Two different types of species have been observed in the complexation process, one of them is a co-ordination complex and the other is a salt generated by ligand deprotonation. The deprotonation reaction induces a conformational change, giving rise to a symmetrical species. This species is responsible for colour development. Ligand 3 has a similar structure and does not give rise to any colour modification due to presence of the dimethylamino groups in the biphenyl moiety. The X-ray structure of ligand 2 is also reported and compared with that of ligand 1, that had bee…

Biphenylchemistry.chemical_classificationConformational changeStereochemistryLigandOrganic ChemistrySalt (chemistry)BiochemistryMedicinal chemistrychemistry.chemical_compoundDeprotonationchemistryDrug DiscoveryMoietyNaked eyeFluorideTetrahedron
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Localization of the N-terminal Domain in Light-harvesting Chlorophyll a/b Protein by EPR Measurements

2005

The conformational distribution of the N-terminal domain of the major light-harvesting chlorophyll a/b protein (LHCIIb) has been characterized by electron-electron double resonance yielding distances between spin labels placed in various domains of the protein. Distance distributions involving residue 3 near the N terminus turned out to be bimodal, revealing that this domain, which is involved in regulatory functions such as balancing the energy flow through photosystems (PS) I and II, exists in at least two conformational states. Models of the conformational sub-ensembles were generated on the basis of experimental distance restraints from measurements on LHCIIb monomers and then checked f…

ChlorophyllModels MolecularThreonineConformational changeTime FactorsLightMacromolecular SubstancesProtein ConformationPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesElectronsTrimerCrystallography X-RayThylakoidsBiochemistryProtein Structure Secondarylaw.inventionResidue (chemistry)chemistry.chemical_compoundlawEscherichia coliAnimalsPhosphorylationAnnexin A4Electron paramagnetic resonanceMolecular BiologyPhotosystemPhotosystem I Protein ComplexChemistryChlorophyll AElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyRecombinant ProteinsProtein Structure TertiaryOxygenN-terminusCrystallographyMonomerThylakoidMutationCattleSpin LabelsDimerizationJournal of Biological Chemistry
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Bovine Serum Albumin protofibril-like aggregates formation: Solo but not simple mechanism

2011

We report an experimental study on the model protein Bovine Serum Albumin (BSA), with the aim of elucidating the mechanisms by which a fully folded globular protein undergoes different aggregation pathways leading to the formation of amyloid fibrils or amorphous aggregates. We observe thermally induced formation of fibrillar structures at pH far from the protein isoelectric point. The increase of electrostatic repulsion results in protein destabilization and in modifications of inter and intra-molecular interactions leading to the growth of fibril-like aggregates stabilized by inter-molecular-β sheets. The aggregation kinetics is studied by means of fluorescence techniques, light scattering…

Circular dichroismProtein ConformationGlobular proteinStatic ElectricityBiophysicsProtein aggregationBiochemistryprotein aggregation amyloid fibril fluorescence conformational changeschemistry.chemical_compoundProtein structureAnimalsBenzothiazolesBovine serum albuminMolecular Biologychemistry.chemical_classificationbiologyTemperatureTryptophanSerum Albumin BovineHydrogen-Ion ConcentrationSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)KineticsThiazolesCrystallographyIsoelectric pointchemistryProtein destabilizationbiology.proteinThermodynamicsCattleThioflavinProtein Multimerization
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A conformationally adaptive macrocycle : conformational complexity and host–guest chemistry of zorb[4]arene

2018

Large amplitude conformational change is one of the features of biomolecular recognition and is also the basis for allosteric effects and signal transduction in functional biological systems. However, synthetic receptors with controllable conformational changes are rare. In this article, we present a thorough study on the host–guest chemistry of a conformationally adaptive macrocycle, namely per-O-ethoxyzorb[4]arene (ZB4). Similar to per-O-ethoxyoxatub[4]arene, ZB4 is capable of accommodating a wide range of organic cations. However, ZB4 does not show large amplitude conformational responses to the electronic substituents on the guests. Instead of a linear free-energy relationship, ZB4 foll…

Conformational changeAllosteric regulationSupramolecular chemistryCrystal structure010402 general chemistry01 natural sciencesHeat capacityFull Research Papersupramolecular chemistrylcsh:QD241-441lcsh:Organic chemistryComputational chemistrysupramolekulaarinen kemiahost-guest chemistryhost–guest chemistrylcsh:ScienceHost–guest chemistryta116010405 organic chemistryChemistryComponent (thermodynamics)Hydrogen bondOrganic Chemistryzorb[4]arene0104 chemical sciencesChemistrymacrocyclesconformationslcsh:QBeilstein Journal of Organic Chemistry
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A density functional theory evaluation of hydrophobic solvation: Ne, Ar and Kr in a 50-water cluster – Implications for the hydrophobic effect

2012

The physical explanation for the hydrophobic effect has been the subject of disagreement. Physical organic chemists tend to use a explanation related to pressure, while many biochemists prefer an explanation that involves decreased entropy of the aqueous solvent. We present DFT calculations at the B3LYP/6-31G(d,p) and X3LYP/6-31G(d,p) levels on the solvation of three noble gases (Ne, Ar, and Kr) in clusters of 50 waters. Vibrational analyses show no substantial decreases in the vibrational entropies of the waters in any of the three clusters. The observed positive free energies of transfer from the gas phase or from nonpolar solvents to water appear to be due to the work needed to make a su…

Conformational changeAqueous solutionChemistrySolvationCondensed Matter PhysicsBiochemistryArticleGas phaseSolventHydrophobic effectChemical physicsComputational chemistryDensity functional theoryWater clusterPhysical and Theoretical ChemistryComputational and Theoretical Chemistry
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