Pressure-induced local unfolding of the Ras binding domain of RalGDS.
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.
Inoue
K
K
Department of Molecular Science, Graduate School of Science and Technology, Kobe University, Kobe 657-8501, Japan.
Yamada
H
H
Akasaka
K
K
Herrmann
C
C
Kremer
W
W
Maurer
T
T
Döker
R
R
Kalbitzer
H R
HR
D001665:Binding Sites; D006874:Hydrostatic Pressure; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D011489:Protein Denaturation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D012997:Solvents; D013816:Thermodynamics; D020726:ral Guanine Nucleotide Exchange Factor / Q000737:chemistry* / Q000378:metabolism*; D018631:ras Proteins / Q000378:metabolism*
D012997:Solvents; D020726:ral Guanine Nucleotide Exchange Factor; D018631:ras Proteins