S El Mohsni

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Conservation of the secondary and tertiary protein organization of human apohemoglobin was observed at temperatures ranging from 7 to 25 degrees C using CD spectra in the far-UV (200-250 nm) and near-UV (250-300 nm) regions. The dynamics of apohemoglobin were probed using fluorescence quenching experiments on the Trp residues and an extrinsic dye (ANS or(More)
Although the fixation of ligand to haemoglobin (Hb) is known to be accompanied by changes in protein conformation regulating the oxygen exchange in blood, the mechanism triggering these changes remains undecided. We now report a dynamic approach to this problem using results obtained in a nanosecond laser photolysis study of carboxyhaemoglobin (HbCO) and(More)
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