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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Using buried water molecules to explore the energy landscape of proteins.

Buried water molecules constitute a highly conserved, integral part of nearly all known protein structures. Such water molecules exchange with external solvent as a result of protein conformational fluctuations. We report here the results of water (17)O and (2)H magnetic relaxation dispersion measurements on wild-type and mutant bovine pancreatic trypsin inhibitor in aqueous solution at 4-80 degrees C. These data lead to the first determination of the exchange rate of a water molecule buried in a protein. The strong temperature dependence of this rate is ascribed to large-scale conformational fluctuations in an energy landscape with a statistical ruggedness of approximately 10 kJ mol(-1).[1]

References

  1. Using buried water molecules to explore the energy landscape of proteins. Denisov, V.P., Peters, J., Hörlein, H.D., Halle, B. Nat. Struct. Biol. (1996) [Pubmed]
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