We argue that, for solutions of immobilized protein and for tissue, the dependence of 1/T1 of solvent protons on B(0) at low fields and 1/T1 rho on B1 for all B(0) are both manifestations of the same underlying phenomena: magnetization transfer between mobile water protons and solid-state broadened protein proton levels. Broadening causes rapid mixing of spin orientation within the transverse plane, at all B(0), unless B1 is greater than the protein internal field; this affects 1/T1 rho of solvent protons by magnetization transfer. Similarly, decreasing B(0) below the internal field mixes all orientations of magnetization, which affects the solvent proton low-field 1/T1 and high-field 1/T2.