1. Dynamics at the Protein-Water Interface from 17O Spin Relaxation in Deeply Supercooled Solutions 
Carlos Mattea, Johan Qvist, Bertil Halle 
Biophysical Journal 
Volume 95, Issue 6, Pages (September 2008)
DOI: /biophysj
Copyright © 2008 The Biophysical Society Terms and Conditions

2. Figure 1
Temperature dependence of different contributions to the water 17O relaxation rate R1 at 81.3MHz for a 5.1mM ubiquitin solution at pH 5.0, plotted on linear (left) and logarithmic (right) scales. The depicted R1 contributions correspond to the three terms in Eq. 1, representing 10,000 bulk water molecules (○), 443 water molecules in the hydration layer (●), and a single internal water molecule (■).
Biophysical Journal  , DOI: ( /biophysj )
Copyright © 2008 The Biophysical Society Terms and Conditions

3. Figure 2
Temperature dependence of the ADPF ξ(ω0,T) at 81.3MHz for BPTI, ubiquitin, and BLG. The contributions from hydration water (light shading) and internal water (dark shading) are indicated. The curves were obtained by fitting the two model parameters ν and EH− (Table 1) to the data (solid circles).
Biophysical Journal  , DOI: ( /biophysj )
Copyright © 2008 The Biophysical Society Terms and Conditions

4. Figure 3
Temperature dependence of the hydration-layer DPF ξH(T,p) for BPTI (solid curves), ubiquitin (dash), and BLG (dash-dot). The three panels show the DPF for all NH hydration waters (left), the 90% most mobile waters (middle), and the 50% most mobile waters (right).
Biophysical Journal  , DOI: ( /biophysj )
Copyright © 2008 The Biophysical Society Terms and Conditions

5. Figure 4
Arrhenius plot showing the mean correlation time 〈τ〉 for the 50% (narrow shaded band) and 90% (wide shaded band) most mobile hydration waters and the correlation time τ0 in bulk water (solid curve). The shaded bands each contain three nearly linear curves for BPTI, ubiquitin, and BLG.
Biophysical Journal  , DOI: ( /biophysj )
Copyright © 2008 The Biophysical Society Terms and Conditions