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Pressure-induced local unfolding of the Ras binding domain of RalGDS

Inoue, K. ; Yamada, H. ; Akasaka, K. ; Herrmann, C. ; Kremer, W. ; Maurer, T. ; Döker, R. ; Kalbitzer, Hans Robert



Abstract

The reliable prediction of the precise three-dimensional structure of proteins from their amino acid sequence is a major, still unresolved problem in biochemistry. Pressure is a parameter that controls folding/unfolding transitions of proteins through the volume change DeltaV of the protein-solvent system. By varying the pressure from 30 to 2,000 bar we detected using 15N/ 1H 2D NMR spectroscopy ...

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