Abstract
Magnetization transfer experiments using an off-resonance irradiation technique were performed on bovine serum albumin solutions by varying the irradiation frequency and the concentration. A transition of the magnetization transfer spectrum from Lorentzian to Gaussian line shape was observed around the critical concentration of 6.2 mmoles of protein to kg of solution. Observed magnetizations were well expressed by the rate equations of populations for spins below and above the transition, which yielded the magnetization transfer rates, the intrinsic relaxation rates of both protein and water protons, and the effective tumbling time and the rigid line width of the protein. The result showed that the estimates of the values for magnetization transfer rate do not change once the critical concentration is reached.
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