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Showing 1 to 5 of 5 for “"carbonmonoxymyoglobin"”.

  1. FTIR studies of environmental effects on carbonmonoxymyoglobin

    "In this thesis, Fourier Transform Infrared Spectroscopy (FTIR) was used to study the interaction between the protein myoglobin (Mb), and substrate carbon-monoxide (CO), as a model system of control in protein-ligand systems. IR spectra of the CO molecule bound to Mb have been obtained as a …

    uiuc Repository record for FTIR studies of environmental effects on carbonmonoxymyoglobin (opens in a new tab)

  2. FTIR studies of environmental effects on carbonmonoxymyoglobin

    In this thesis, Fourier Transform Infrared Spectroscopy (FTIR) was used to study the interaction between the protein myoglobin (Mb), and substrate carbon-monoxide (CO), as a model system of control in protein-ligand systems. IR spectra of the CO molecule bound to Mb have been obtained as a function …

    uiuc Repository record for FTIR studies of environmental effects on carbonmonoxymyoglobin (opens in a new tab)

  3. Long lived states induced by extended illumination of carbonmonoxy-myoglobin

    … kinetics of recombination of photodissociated carbonmonoxymyoglobin are non-exponential, having amplitude components that extend over many orders of magnitude in time. The bound and unbound states of the system have different spectroscopic signatures and the kinetics of recombination can be …

    uiuc Repository record for Long lived states induced by extended illumination of carbonmonoxy-myoglobin (opens in a new tab)

  4. Multinuclear NMR Studies of Hemoproteins and Their Model Compounds

    … first iron-57 NMR spectra of a metalloprotein, carbonmonoxymyoglobin, has been obtained, yielding the isotropic chemical shift, the anisotropy of the chemical shielding tensor and the rotational correlation time of the protein. The oxygen-17 NMR signals from CO ligands bound to oxygen-transport …

    uiuc Repository record for Multinuclear NMR Studies of Hemoproteins and Their Model Compounds (opens in a new tab)

  5. Motions in myoglobin

    … some of these protein motions. Sperm whale carbonmonoxymyoglobin exhibits three spectroscopically distinguishable carbon monoxide stretch bands between 1910 cm-1 and 1990 cm-1 labeled A0 , Ah and A3 . Pressure release measurements reveal three relaxations in the protein which are measured …

    uiuc Repository record for Motions in myoglobin (opens in a new tab)