Dynamics at the protein-water interface from 17O spin relaxation in deeply supercooled solutions.

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 J

journal_title

Biophysical journal

authors

Mattea C,Qvist J,Halle B

doi

10.1529/biophysj.108.135194

subject

Has Abstract

pub_date

2008-09-15 00:00:00

pages

2951-63

issue

6

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(08)78436-4

journal_volume

95

pub_type

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