Origins of apparent fragile-to-strong transitions of protein hydration waters.

2H 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 approximately 225 K (X1) and Tx2 approximately 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.