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New clues to how proteins dissolve and crystallize
Date:5/12/2008

ty and allowing the protein to precipitate," he says. "But a more modern view is emerging, one exemplified by the Law of Matching Water Affinities, which suggests that Hofmeister effects are not due to such long-range perturbations of water but instead operate at a very short range, over a distance of only one or two molecules."

Of the dominant biological cations, for example, calcium and sodium are weak kosmotropes and potassium is a weak chaotrope. Says Saykally, "What matters is not whether individual cations are kosmotropes or chaotropes but how closely they are matched when they pair up with anions -- whether, in terms of hydration energy, they are two of a kind."

By using liquid microjet technology and x-ray absorption spectroscopy to characterize how sodium, potassium, and lithium interact with carboxylate groups, which are among the dominant anions in biological systems (and themselves kosmotropes), Saykally and his colleague have opened a new path toward probing selective interactions of ions with biological molecules in the aqueous environments typical of their natural surroundings. And they have gained new insight into the workings of the Hofmeister series, which has been called "as important to protein chemistry as Mendel was to genetics."


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Contact: Paul Preuss
paul_preuss@lbl.gov
510-486-6249
DOE/Lawrence Berkeley National Laboratory
Source:Eurekalert  

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