Abstract
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 17O and 2H magnetic relaxation dispersion measurements on wild-type and mutant bovine pancreatic trypsin inhibitor in aqueous solution at 4–80 °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 ∼10 kJ mol−1.
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Denisov, V., Peters, J., Hörlein, H. et al. Using buried water molecules to explore the energy landscape of proteins. Nat Struct Mol Biol 3, 505–509 (1996). https://doi.org/10.1038/nsb0696-505
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DOI: https://doi.org/10.1038/nsb0696-505
