Abstract
H2 NMR is used to study the mechanisms for the reorientation of protein hydration water. In the past, crossovers in temperature-dependent correlation times were reported at Tx1≈225  K (X1) and Tx2≈200  K (X2). We show that neither X1 nor X2 are related to a fragile-to-strong transition. Our results rule out an existence of X1. Also, they indicate that water performs thermally activated and distorted tetrahedral jumps at T<Tx2, implying that X2 originates in an onset of this motion, which may be related to a universal defect diffusion in materials with defined hydrogen-bond networks.