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

Autor:	K, Inoue, H, Yamada, K, Akasaka, C, Herrmann, W, Kremer, T, Maurer, R, Döker, H R, Kalbitzer
Rok vydání:	2000
Předmět:	Models Molecular Protein Denaturation Protein Folding Binding Sites ral Guanine Nucleotide Exchange Factor Hydrostatic Pressure Solvents ras Proteins Thermodynamics Nuclear Magnetic Resonance Biomolecular Protein Binding Protein Structure Tertiary
Zdroj:	Nature structural biology. 7(7)
ISSN:	1072-8368
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::5f793a90ea0ff0ba83769fb43239e1e2 https://pubmed.ncbi.nlm.nih.gov/10876238 Zobrazit plný text záznamu Plný text ve formátu PDF