Search results for "Carboxymyoglobin"

showing 6 items of 6 documents

Bioprotection Can Be Tuned with Proper Protein/Saccharide Ratio: The Case of Solid Amorphous Matrices

2018

Saccharides, and in particular trehalose, are well known for their high efficiency in protecting biostructures against adverse environmental conditions. The protein dynamics is known to be highly inhibited in a low-water trehalose host medium, the inhibition being markedly dependent on the amount of residual water. Besides hydration, the protein/sugar ratio is expected to affect the properties of saccharide amorphous matrices. In this work, we report an infrared spectroscopy study in dry amorphous matrices of various sugars (the disaccharides trehalose, maltose, sucrose, and lactose, and the trisaccharide raffinose) containing myoglobin, at different protein/sugar ratios. We analyze the str…

0301 basic medicineSucrose010402 general chemistry01 natural sciences03 medical and health scienceschemistry.chemical_compoundSpectroscopy Fourier Transform InfraredMaterials ChemistryTrisaccharidePhysical and Theoretical ChemistryRaffinoseTrehalose carboxymyoglobin infrared spectroscopySugarchemistry.chemical_classificationCarbon MonoxideMolecular StructureMyoglobinWaterMaltoseTrehaloseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical sciencesSurfaces Coatings and FilmsAmorphous solid030104 developmental biologychemistryMyoglobinChemical engineeringSugars
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Coupling between the Thermal Evolution of the Heme Pocket and the External Matrix Structure in Trehalose Coated Carboxymyoglobin

2003

Proteins can assume a very large number of conformations (conformational substates), all concurring to its function. We present experimental evidence for the existence, in trehalose coated carboxymyoglobin, of a structured environment of the protein, tightly coupled to the heme pocket structure, as experienced by the bound CO molecule. This was evidenced by the strict correlation observed between the thermal evolution (300−20 K) of the CO stretching and of the water association bands in samples of carboxymyoglobin embedded in trehalose matrixes of different hydration. This observation put forward the coupling between the degrees of freedom of the matrix and those of the protein. In the drie…

ChemistryTrehaloseTemperature inducedSurfaces Coatings and FilmsCoupling (electronics)chemistry.chemical_compoundCrystallographyMatrix (mathematics)CarboxymyoglobinThermalMaterials ChemistryMoleculePhysical and Theoretical ChemistryHemeThe Journal of Physical Chemistry B
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Thermal Behavior of dry and hydrated MbCO crowded systems

2009

Crowding carboxymyoglobin protein-matrix coupling FTIR
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MbCO↔matrix reciprocal effects in low hydration amorphous saccharide systems: a FTIR study

2009

trehalose carboxymyoglobin FTIR bioprotection
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SAXS and FTIR study on MbCO-Saccharide amorphous systems

2009

trehalose carboxymyoglobin SAXS FTIR bioprotection
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FTIR Study on Reciprocal Protein↔Matrix effects in dry amorphous saccharide systems

2009

trehalose saccharide carboxymyoglobin FTIR biopreservation
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