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

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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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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Item Type:Article
Date:2000
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
10876238PubMed ID
10.1038/76764DOI
Classification:
NotationType
Binding SitesMESH
Hydrostatic PressureMESH
Models, MolecularMESH
Nuclear Magnetic Resonance, BiomolecularMESH
Protein BindingMESH
Protein DenaturationMESH
Protein FoldingMESH
Protein Structure, TertiaryMESH
SolventsMESH
ThermodynamicsMESH
ral Guanine Nucleotide Exchange Factor/metabolismMESH
ras Proteins/metabolismMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:15 Sep 2010 09:00
Last Modified:15 Sep 2010 09:00
Item ID:16571
Owner Only: item control page
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