T1ρ of protein solutions at very low fields: Dependence on molecular weight, concentration, and structure

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Abstract
The effect of molecular weight, concentration, and structure on 1/T1ρ, the rotating frame relaxation rate, was investigated for several proteins using the on-resonance spin-lock technique, for locking fields B1 < 200 μT. The measured values of 1/T1ρ, were fitted to a simple theoretical model to obtain the dispersion curves 1/T1ρ(ω1) and the relaxation rate at zero B1 field, 1/T1ρ,(O). 1/T1ρ, was highly sensitive to the molecular weight, concentration, and structure of the protein. The amount of intra- and intermolecular hydrogen and disulfide bonds especially contributed to 1/T1ρ. In all samples, 1/T1ρ(O) was equal to 1/T2ρ measured at the main magnetic field Bo = 0.1 T, but at higher locking fields the dispersion curves mono-tonically decreased. The results of this work indicate that a model considering the effective correlation time of molecular motions as the main determinant for 1/T1ρ relaxation in protein solutions is not valid at very low B1 fields. The underlying mechanism for the relaxation rate 1/T1ρ at B1 fields below 200 μT is discussed.