Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Pressure-induced local unfolding of the Ras binding domain of RalGDS.

Literature DB >> 10876238

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

K Inoue¹, H Yamada, K Akasaka, C Herrmann, W Kremer, T Maurer, R Döker, H R Kalbitzer.

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.

Entities: Chemical Gene

Mesh：

Substances：

Year: 2000 PMID： 10876238 DOI： 10.1038/76764

Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368

Keyword Cloud
Cited

18 in total

1. A model of the pressure dependence of the enantioselectivity of Candida rugosalipase towards (+/-)-menthol.

Authors: U H Kahlow; R D Schmid; J Pleiss
Journal: Protein Sci Date: 2001-10 Impact factor: 6.725

2. Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding.

Authors: Ryo Kitahara; Kazuyuki Akasaka
Journal: Proc Natl Acad Sci U S A Date: 2003-03-10 Impact factor: 11.205

3. High-pressure 1H NMR study of pressure-induced structural changes in the heme environments of metcyanomyoglobins.

Authors: Ryo Kitahara; Minoru Kato; Yoshihiro Taniguchi
Journal: Protein Sci Date: 2003-02 Impact factor: 6.725

4. Revealing conformational substates of lipidated N-Ras protein by pressure modulation.

Authors: Shobhna Kapoor; Gemma Triola; Ingrid R Vetter; Mirko Erlkamp; Herbert Waldmann; Roland Winter
Journal: Proc Natl Acad Sci U S A Date: 2011-12-27 Impact factor: 11.205

5. Cavity as a source of conformational fluctuation and high-energy state: high-pressure NMR study of a cavity-enlarged mutant of T4 lysozyme.

Authors: Akihiro Maeno; Daniel Sindhikara; Fumio Hirata; Renee Otten; Frederick W Dahlquist; Shigeyuki Yokoyama; Kazuyuki Akasaka; Frans A A Mulder; Ryo Kitahara
Journal: Biophys J Date: 2015-01-06 Impact factor: 4.033

10. Key stabilizing elements of protein structure identified through pressure and temperature perturbation of its hydrogen bond network.

Authors: Lydia Nisius; Stephan Grzesiek
Journal: Nat Chem Date: 2012-07-08 Impact factor: 24.427

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

1. A model of the pressure dependence of the enantioselectivity of Candida rugosalipase towards (+/-)-menthol.

2. Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding.

3. High-pressure 1H NMR study of pressure-induced structural changes in the heme environments of metcyanomyoglobins.

4. Revealing conformational substates of lipidated N-Ras protein by pressure modulation.

5. Cavity as a source of conformational fluctuation and high-energy state: high-pressure NMR study of a cavity-enlarged mutant of T4 lysozyme.

6. Pressure-Temperature Analysis of the Stability of the CTL9 Domain Reveals Hidden Intermediates.

7. Pressure response of amide one-bond J-couplings in model peptides and proteins.

8. Monitoring ¹⁵N Chemical Shifts During Protein Folding by Pressure-Jump NMR.

9. Water-Protein Interactions Coupled with Protein Conformational Transition.

10. Key stabilizing elements of protein structure identified through pressure and temperature perturbation of its hydrogen bond network.