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

Inoue, Kyoko and Yamada, Hiroaki and Akasaka, Kazuyuki and Herrmann, Christian and Kremer, Werner and Maurer, Till and Döker, Rolf and Kalbitzer, Hans Robert (2000) Pressure-induced local unfolding of the Ras binding domain of RalGDS. NATURE STRUCTURAL BIOLOGY, 7 (7). pp. 547-550. ISSN 1072-8368

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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 Delta V of the protein-solvent system. By varying the pressure from 30 to 2,000 bar we detected using N-15/H-1 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.

Item Type: Article
Uncontrolled Keywords: CHEMICAL-SHIFTS; HIGH-RESOLUTION; NMR; PROTEINS; H-1; DENATURATION; SENSITIVITY; DEPENDENCE; LYSOZYME; DYNAMICS
Subjects: 500 Science > 570 Life sciences
Divisions: Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Depositing User: Dr. Gernot Deinzer
Date Deposited: 24 Aug 2023 09:31
Last Modified: 24 Aug 2023 09:31
URI: https://pred.uni-regensburg.de/id/eprint/42366

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