SynopsisThe dynamic behavior of pig immunoglobulin G in deuterium oxide solutions was investigated by the neutron spin-echo technique. This novel technique makes it possible to study intramolecular motion without introducing probes into the macromolecule.Using neutron spin-echo, the effective diffusion coefficient, Deff, was obtained as a function of the transferred momentum, K. For interpretation of the experimental data, two models were designed, and computed Dew values were compared with experimental data.The rigid T-shape model was compatible with the experimental data only by assuming an unrealistically high rotational diffusion coefficient, and it was therefore unacceptable. Reasonable agreement with all available experimental data was obtained with a flexible model of immunoglobulin G molecule, which the Fab arms are assumed to wobble around the hinge region within an angle of 50".
On a étudié par spectrométrie Môssbauer, entre 4,2 K et 200 K, de l'hémoglobine déoxygénée, enrichie au 57 Fe, d'un homme adulte (HbA), ses chaînes isolées as H et /?SH et de l'hémoglobine totale a2(57 Fe) /?2(56 Fe) partiellement enrichie en 57 Fe. Compte tenu de la précision expérimentale (± 0,006 mm s-1) l'effet quadrupolaire des HbA des chaînes asir et /3SH varie entre 100 K et 4,2 K ; de plus l'effet quadrupolaire de HbA n'est pas la moyenne des valeurs trouvées pour les chaînes isolées. L'effet quadrupolaire de a2(57 Fe) /?2(56 Fe) est pratiquement le même que celui de HbA. Les mêmes tendances sont retrouvées sur les valeurs du déplacement isomérique. Les largeurs de raies ont des valeurs très voisines pour tous les composés.
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