Search results for "Globin"

showing 10 items of 734 documents

An unambiguous procedure for discovering relaxation influence on M�ssbauer spectra

1994

A mathematical procedure which gives an opportunity to distinguish between relaxation and distribution mechanisms of the Mossbauer line broadening is proposed. It is based on the method of Mossbauer line sharpening developed recently [1] and allows one to answer unambiguously the question whether or not relaxation manifests itself in Mossbauer measurements by examining the wings of the spectrum. The procedure is applied to the spectra of high spin ferric metmyoglobin and (Fe0.65Ni0.35)1−xMnx alloys. Analysis of the metmyoglobin spectra manifests the presence of the relaxation influence in the temperature range 10 K≦T≦100 K. Analysis of the alloy spectra shows that for the temperatures 4 K≦T…

Materials scienceMössbauer effectCondensed Matter PhysicsSpectral lineElectronic Optical and Magnetic MaterialsNuclear magnetic resonanceMetmyoglobinMössbauer spectroscopyRelaxation (physics)General Materials ScienceAtomic physicsSpin (physics)Hyperfine structureLine (formation)Zeitschrift f�r Physik B Condensed Matter
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Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering

2008

We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.

Materials scienceProtein ConformationCrystallography X-RayBiochemistrySensitivity and SpecificityArticlechemistry.chemical_compoundHemoglobinsProtein structureScattering RadiationSpectroscopyWide-angle X-ray scatteringMolecular Biologyprotein dynamics conformational changes hemoglobin myoglobin cytochrome cScatteringMyoglobinX-RaysResolution (electron density)Cytochromes cCell BiologyNanosecondMyoglobinchemistryChemical physicsProtein quaternary structuresense organsBiotechnology
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Aptamer-embedded DNA origami cage for detecting (glycated) hemoglobin with a surface plasmon resonance sensor

2020

DNA origami-based cages functionalized with aptamer motifs, were used to detect hemoglobin and glycated hemoglobin. The binding between the cages and hemoglobin was monitored using a surface plasmon resonance (SPR) sensor. One DNA strand in the nano-cage was replaced with an aptamer that demonstrated a high affinity to hemoglobin (Hb) or glycated hemoglobin (gHb). Three types of the DNA nano-cages designed to fit the size and shape of hemoglobin were evaluated: one without an aptamer, one with the Hb-affinity aptamer (HA) and one with the gHb-affinity aptamer (GHA). Both DNA nano-cages embedded with HA and GHA showed significantly more stable binding with Hb and gHb by 5 and 9 times, respec…

Materials scienceSurface plasmon resonance sensorAptamerAptamerDissociation constant02 engineering and technologybiosensorit010402 general chemistry01 natural sciencesSurface plasmon resonance sensorchemistry.chemical_compoundGlycated hemoglobinnanorakenteethemoglobiiniDNA origamiGeneral Materials ScienceSurface plasmon resonanceMechanical EngineeringDNA021001 nanoscience & nanotechnologyCondensed Matter Physics0104 chemical sciencesplasmonitDissociation constantchemistryMechanics of MaterialsBiophysicsDNA origamiHemoglobinGlycated hemoglobin0210 nano-technologyDNAMaterials Letters
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RGB imaging system for mapping and monitoring of hemoglobin distribution in skin

2011

A prototype R-G-B imaging system for mapping of skin hemoglobin distribution has been designed and tested. Device basically consists of a commercial RGB sensor (CMOS, max. frame rate 87 fps for VGA resolution), RGB LED ringlight illuminator and orthogonally orientated polarizers for reducing specular reflectance. The system was examined for monitoring of hemoglobin concentration changes during specific provocations - arterial/venous occlusions and heat test. Hemoglobin distribution maps of several skin malformations were obtained, as well.

Materials scienceVideo Graphics Arraybusiness.industryPolarizerFrame rateReflectivitylaw.inventionOpticslawRGB color modelComputer visionHemoglobinSpecular reflectionArtificial intelligencebusinessSPIE Proceedings
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OXYGEN SOLUBILITY IN NORMAL HUMAN BLOOD

1981

Publisher Summary This chapter describes oxygen solubility in normal human blood. The most crucial problem in measuring physically dissolved oxygen in blood is the prevention of oxygen binding by hemoglobin (Hb). The chapter discusses a study for the re-determination of oxygen solubility in untreated human blood. The oxygen concentration was measured by a photometric method and the Hb-concentration was determined by the cyanohemoglobin method. Oxygen solubility in normal and untreated blood is a linear function of the Hb-concentration. Hemoglobin in the reduced state has a greater influence on oxygen solubility than hemoglobin. Red cell membranes have no measureable effect on the oxygen sol…

MembraneChromatographyRed CellHuman bloodChemistryLimiting oxygen concentrationHemoglobinCyanohemoglobinOxygen solubilityOxygen binding
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Diagnostic use of fructosamine assay in the control of type II diabetes mellitus.

1988

In an attempt to evaluate the usefulness of fructosamine assay in monitoring type II diabetes, 142 diabetic patients were investigated. Fructosamine values were found to be higher in patients on insulin treatment than on oral hypoglycemic agents. In order to evaluate the metabolic control by using the correlated variations of F, Gm and HbAlc, the patients were subdivided into many control classes: mean values of fructosamine were higher in poorly controlled patients. Fructosamine however correlated better with glycemia in patients with recent variations in metabolic state than HbAlc. It was concluded that fructosamine is a good index for short-term metabolic control, and if used in an integ…

Metabolic stateAdultBlood GlucoseMalemedicine.medical_specialtyEndocrinology Diabetes and Metabolismmedicine.medical_treatmentGastroenterologyType ii diabeteschemistry.chemical_compoundEndocrinologyPhenforminReference ValuesDiabetes mellitusInternal medicineGlyburideInternal MedicineMedicineHumansInsulinIn patientGlycated Hemoglobinbusiness.industryInsulinHexosaminesGeneral MedicineMiddle Agedmedicine.diseaseFructosamineEndocrinologychemistryDiabetes Mellitus Type 2Metabolic control analysisOral hypoglycemic agentsFructosamineFemalebusinessActa diabetologica latina
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Internal dynamics and protein-matrix coupling in trehalose-coated proteins.

2005

Abstract We review recent studies on the role played by non-liquid, water-containing matrices on the dynamics and structure of embedded proteins. Two proteins were studied, in water–trehalose matrices: a water-soluble protein (carboxy derivative of horse heart myoglobin) and a membrane protein (reaction centre from Rhodobacter sphaeroides ). Several experimental techniques were used: Mossbauer spectroscopy, elastic neutron scattering, FTIR spectroscopy, CO recombination after flash photolysis in carboxy-myoglobin, kinetic optical absorption spectroscopy following pulsed and continuous photoexcitation in Q B containing or Q B deprived reaction centre from R. sphaeroides . Experimental result…

Models MolecularAbsorption spectroscopyPhotosynthetic Reaction Center Complex ProteinsBiophysicsHemeRhodobacter sphaeroidesNeutron scatteringBiochemistryAnalytical Chemistrychemistry.chemical_compoundRhodobacter sphaeroidesMolecular dynamicsSpectroscopy Fourier Transform InfraredComputer SimulationMolecular Biologytrehalose protein simulation spectroscopyPhotolysisbiologyHydrogen bondMyoglobinTemperatureTrehaloseWaterHydrogen Bondingbiology.organism_classificationCrystallographyKineticsMyoglobinchemistryMembrane proteinFlash photolysisBiochimica et biophysica acta
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Hemocyanin from E. californicum encapsulated in silica gels: oxygen binding and conformational states.

2007

Cooperativity depends on the existence of equilibria among functionally distinct conformational states that are affected by homo and heterotropic effectors. In order to isolate the quaternary conformations of hemocyanin from E. californicum, the 24-meric giant protein was encapsulated in wet, nanoporous silica gels, either in the absence or presence of oxygen. The deoxy- and oxy-hemocyanin gels exhibit a p50 for oxygen of 11 and 2.5 torr, respectively, values in close agreement with those for hemocyanin in solution. The observed Hill coefficients are lower than unity, indicating a conformational heterogeneity within each locked conformational state, a finding in agreement with the assumptio…

Models MolecularAbsorption spectroscopyProtein Conformationmedicine.medical_treatmentchemistry.chemical_elementCooperativityBiologyOxygenGeneticsmedicineAnimalsNanoporousHemocyaninSpidersGeneral MedicineSilicon DioxideOxygenSolutionsCrystallographyKineticsBiochemistrychemistrySpectrophotometryHemocyaninsHemoglobinGelsOxygen bindingAlgorithmsProtein BindingGene
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Crystal Structure of Cytoglobin: The Fourth Globin Type Discovered in Man Displays Heme Hexa-coordination

2004

Cytoglobin is a recently discovered hemeprotein belonging to the globin superfamily together with hemoglobin, myoglobin and neuroglobin. Although distributed in almost all human tissues, cytoglobin has not been ascribed a specific function. Human cytoglobin is composed of 190 amino acid residues. Sequence alignments show that a protein core region (about 150 residues) is structurally related to hemoglobin and myoglobin, being complemented by about 20 extra residues both on the N and C termini. In the absence of exogenous ligands (e.g. O2), the cytoglobin distal HisE7 residue is coordinated to the heme Fe atom, thus decreasing the ligand affinity. The crystal structure of human cytoglobin (2…

Models MolecularHemeproteinStereochemistryMolecular Sequence DataHemeCrystallography X-RayProtein Structure Secondarychemistry.chemical_compoundProtein structureStructural BiologyAnimalsHumansAmino Acid SequenceGlobinMolecular BiologyHemeBinding SitesCytoglobinCytoglobinOxygen transportGlobinsProtein Structure TertiaryGlobin foldBiochemistrychemistryMyoglobinSequence AlignmentJournal of Molecular Biology
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Molecular dynamics simulation of sucrose- and trehalose-coated carboxy-myoglobin

2005

We performed a room temperature molecular dynamics (MD) simulation on a system containing 1 carboxy-myoglobin (MbCO) molecule in a sucrose–water matrix of identical composition (89% [sucrose/(sucrose + water)] w/w) as for a previous trehalose–water–MbCO simulation (Cottone et al., Biophys J 2001;80:931–938). Results show that, as for trehalose, the amplitude of protein atomic mean-square fluctuations, on the nanosecond timescale, is reduced with respect to aqueous solutions also in sucrose. A detailed comparison as a function of residue number evidences mobility differences along the protein backbone, which can be related to a different efficacy in bioprotection. Different heme pocket struc…

Models MolecularInfrared spectroscopyDisaccharidesBiochemistrychemistry.chemical_compoundMolecular dynamicsStructural BiologyCarbohydrate ConformationMoleculeComputer Simulationheme pocket; hydrogen bond; mean-square fluctuations; protein dynamics; sucrose; trehaloseheme pocketMolecular Biologytrehalosehydrogen bondAqueous solutionBinding SitesHydrogen bondMyoglobinProtein dynamicssucroseTrehaloseCrystallographyKineticschemistryMyoglobinprotein dynamicsmolecular dynamics myoglobin disaccharidemean-square fluctuations
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