title: Pressure-induced local unfolding of the Ras binding domain of RalGDS.
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 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.
authors.affiliation: Department of Molecular Science, Graduate School of Science and Technology, Kobe University, Kobe 657-8501, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Inoue
authors.forename: H
authors.initials: H
authors.lastname: Yamada
authors.forename: K
authors.initials: K
authors.lastname: Akasaka
authors.forename: C
authors.initials: C
authors.lastname: Herrmann
authors.forename: W
authors.initials: W
authors.lastname: Kremer
authors.forename: T
authors.initials: T
authors.lastname: Maurer
authors.forename: R
authors.initials: R
authors.lastname: Döker
authors.forename: H R
authors.initials: HR
authors.lastname: Kalbitzer
mesh_terms: 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*
chemical_list: D012997:Solvents; D020726:ral Guanine Nucleotide Exchange Factor; D018631:ras Proteins