Go to content
UR Home

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

Inoue, K., Yamada, H., Akasaka, K., Herrmann, C., Kremer, W., Maurer, T., 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.

Full text not available from this repository.

at PubMed

at publisher (via DOI)


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 ...

plus


Export bibliographical data



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
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Item ID:16571
Owner only: item control page
  1. Homepage UR

University Library

Publication Server

Contact:

Publishing: oa@ur.de

Dissertations: dissertationen@ur.de

Research data: daten@ur.de

Contact persons