Search results for "MbCO"

showing 4 items of 4 documents

Myoglobin embedded in saccharide amorphous matrices: water-dependent domains evidenced by small angle X-ray scattering

2010

We report Small Angle X-ray Scattering (SAXS) measurements performed on samples of carboxy-myoglobin (MbCO) embedded in low-water trehalose glasses. Results showed that, in such samples, "low-protein" trehalose-water domains are present, surrounded by a protein-trehalose-water background; such finding is supported by Infrared Spectroscopy (FTIR) measurements. These domains, which do not appear in the absence of the protein and in analogous sucrose systems, preferentially incorporate the incoming water at the onset of rehydration, and disappear following large hydration. This observation suggests that, in organisms under anhydrobiosis, analogous domains could play a buffering role against th…

Photosynthetic reaction centreSucroseGLASS-TRANSITIONGeneral Physics and AstronomyInfrared spectroscopyRhodobacter sphaeroideschemistry.chemical_compoundRhodobacter sphaeroidesScattering Small AngleSpectroscopy Fourier Transform InfraredPHOSPHOLIPID-BILAYERREACTION CENTERSPhysical and Theoretical ChemistrySettore CHIM/02 - Chimica FisicabiologyScatteringSmall-angle X-ray scatteringMyoglobinTrehaloseWaterbiology.organism_classificationPROTEIN DYNAMICSTrehaloseMOLECULAR-DYNAMICS SIMULATIONAmorphous solidCrystallographyMyoglobinchemistryTHERMAL-DENATURATIONNEUTRON-SCATTERINGCARBOXY-MYOGLOBINEXTERNAL MATRIXTREHALOSE-COATED MBCO
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MbCO embedded in trehalosyldextrin matrices: thermal effects and protein-matrix coupling

2010

Saccharide-based biopreservation is widely studied because of its scientific importance and possible technological outcomes for food and pharmaceutical industries. Ternary protein/saccharide/water systems have been extensively exploited to model the characteristics of the in vivo biopreservation process. A tight, water dependent, protein–matrix coupling has been shown to occur in various simple saccharide amorphous matrices, which is stronger in trehalose. The efficiency as bioprotectant of trehalose has been ascribed to this tight coupling, since the appearance of damages on biological structures will more involve structural variations of the surrounding matrix. Here we present, as an appl…

chemistry.chemical_classificationdenaturationBiophysicsInfrared spectroscopyTrehaloseBioengineeringApplied Microbiology and BiotechnologyTrehaloseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Analytical ChemistryAmorphous solidchemistry.chemical_compoundMatrix (mathematics)chemistryChemical engineeringOrganic chemistryDenaturation (biochemistry)DextrinFourier transform infrared spectroscopyTernary operationMbCOdextrinInfrared spectroscopyFood ScienceSettore CHIM/02 - Chimica Fisica
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Protein-Matrix Coupling in MbCO embedded in saccharide matrices

2008

saccharideIRcouplingMbCOtrehaloseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Settore CHIM/02 - Chimica Fisica
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MbCo in Saccharide Solid Amorphous Systems: A Combined FTIR and SAXS Study

2011

Saccharides, and in particular trehalose, are known for their efficiency in protecting biostructures against environmental stress [1], although the preservation mechanism is still debated. Experiments and simulations [2,3] on carboxy-myoglobin (MbCO) showed that the protein dynamics is highly inhibited in dry trehalose matrices, the inhibition being dependent on the water content. In these conditions, a mutual protein-matrix structural and dynamic influence is observed.Here we report a combined FTIR and SAXS study on MbCO embedded in dry amorphous matrices of trehalose and sucrose. FTIR measurements were performed at different protein/sugar ratios, focussing on the stretching band of the bo…

saccharideSucroseSmall-angle X-ray scatteringdenaturationProtein dynamicsBiophysicsTrehaloseEnvironmental stressAmorphous solidsmall-angle scatteringchemistry.chemical_compoundCrystallographychemistryFourier transform infrared spectroscopyinfrared spectrocopySugarMbCO
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