Abstract:
:Most of the decisive molecular events in biology take place at the protein-water interface. The dynamical properties of the hydration layer are therefore of fundamental importance. To characterize the dynamical heterogeneity and rotational activation energy in the hydration layer, we measured the (17)O spin relaxation rate in dilute solutions of three proteins in a wide temperature range extending down to 238 K. We find that the rotational correlation time can be described by a power-law distribution with exponent 2.1-2.3. Except for a small fraction of secluded hydration sites, the dynamic perturbation in the hydration layer is the same for all proteins and does not differ in any essential way from the hydration shell of small organic solutes. In both cases, the dynamic perturbation factor is <2 at room temperature and exhibits a maximum near 262 K. This maximum implies that, at low temperatures, the rate of water molecule rotation has a weaker temperature dependence in the hydration layer than in bulk water. We attribute this difference to the temperature-independent constraints that the protein surface imposes on the water H-bond network. The free hydration layer studied here differs qualitatively from confined water in solid protein powder samples.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Mattea C,Qvist J,Halle Bdoi
10.1529/biophysj.108.135194subject
Has Abstractpub_date
2008-09-15 00:00:00pages
2951-63issue
6eissn
0006-3495issn
1542-0086pii
S0006-3495(08)78436-4journal_volume
95pub_type
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