Inoue, K. and Yamada, H. and Akasaka, K. and Herrmann, C. and Kremer, W. and Maurer, T. and Döker, R. and Kalbitzer, Hans Robert (2000) Pressure-induced local unfolding of the Ras binding domain of RalGDS. Nature structural biology 7 (7), pp. 547-550.
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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 a unique equilibrium unfolding intermediate I in the Ras binding domain of the Ral guanine nucleotide dissociation stimulator (Ral GDS). It is characterized by a local melting of specific structural elements near hydrophobic cavities while the overall folded structure is maintained.
|Institutions:||Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer|
|Subjects:||500 Science > 570 Life sciences|
|Created at the University of Regensburg:||Unknown|
|Deposited On:||15 Sep 2010 11:00|
|Last Modified:||15 Sep 2010 11:00|
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