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Default (2)H NMR study of the water dynamics in hydrated myoglobin.

(2)H NMR study of the water dynamics in hydrated myoglobin.

Related Articles (2)H NMR study of the water dynamics in hydrated myoglobin.

J Phys Chem B. 2010 Aug 12;114(31):10209-16

Authors: Lusceac SA, Vogel M

We use 1D and 2D (2)H NMR to study the temperature-dependent mechanism for the rotational motion of myoglobin hydration water. The results show that isotropic and anisotropic water reorientation is observed at high and low temperatures, respectively, with a continuous crossover in the temperature range of 200-230 K. The anisotropic low-temperature motion has a large angular amplitude. It exhibits a broad distribution of geometries and pronounced dynamical heterogeneities, which are long-lived at least at T approximately 176 K. Exploiting the possibility to vary the angular resolution of (2)H NMR experiments, we find that the large solid angle accessible to low-temperature water reorientation is explored via large-angle rather than small-angle elementary steps; i.e., the rotational motion is not diffusive. Quantitative analysis of the NMR data using random-walk simulations implies that the number of sites involved in the observed water reorientation decreases from an infinite number during essentially isotropic motion above 230 K to a few, possibly two, below 165 K. Although the changes in the mechanism for water rotational motion may be accompanied by a mild change in the temperature dependence of the rotational correlation times, the (2)H NMR data provide strong evidence against the existence of a sharp fragile-to-strong transition at about 225 K. The present results are discussed in the context of previous experimental findings for hydrated proteins.

PMID: 20684645 [PubMed - in process]



Source: PubMed
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