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Literature DB >> 20153

Nuclear magnetic resonance studies of the denaturation of ubiquitin.

R E Lenkinski, D M Chen, J D Glickson, G Goldstein.

Abstract

The effects of pH, temperature and guanidine hydrochloride concentration on the structure of ubiquitin, a polypeptide which can activate adenylate cyclase and can mimic thymopoietin induced differentiation of prothymocytes, were monitored using nuclear magnetic resonance spectroscopy. This relatively small polypeptide (molecular weight of 8541) exhibits a remarkable stability towards pH and temperature changes. At 7 M guanidine hydrochloride concentration, the structure of ubiquitin is essentially a random coil.

Entities: Chemical

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Year: 1977 PMID： 20153 DOI： 10.1016/0005-2795(77)90140-4

Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002

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Cited

30 in total

1. The role of a beta-bulge in the folding of the beta-hairpin structure in ubiquitin.

Authors: P Y Chen; B G Gopalacushina; C C Yang; S I Chan; P A Evans
Journal: Protein Sci Date: 2001-10 Impact factor: 6.725

Review 2. Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes.

Authors: Min Jae Lee; Byung-Hoon Lee; John Hanna; Randall W King; Daniel Finley
Journal: Mol Cell Proteomics Date: 2010-09-07 Impact factor: 5.911

3. Observation of protein folding/unfolding dynamics of ubiquitin trapped in agarose gel by single-molecule FRET.

Authors: Li-Ling Yang; Michael W-P Kao; Hsin-Liang Chen; Tsong-Shin Lim; Wunshain Fann; Rita P-Y Chen
Journal: Eur Biophys J Date: 2011-11-09 Impact factor: 1.733

4. Motional properties of unfolded ubiquitin: a model for a random coil protein.

Authors: Julia Wirmer; Wolfgang Peti; Harald Schwalbe
Journal: J Biomol NMR Date: 2006-07 Impact factor: 2.835

5. Conformation types of ubiquitin [M+8H]8+ Ions from water:methanol solutions: evidence for the N and A States in aqueous solution.

Authors: Huilin Shi; Nicholas A Pierson; Stephen J Valentine; David E Clemmer
Journal: J Phys Chem B Date: 2012-03-02 Impact factor: 2.991

6. Molecular dynamics simulations of the native and partially folded states of ubiquitin: influence of methanol cosolvent, pH, and temperature on the protein structure and dynamics.

Authors: David B Kony; Philippe H Hünenberger; Wilfred F van Gunsteren
Journal: Protein Sci Date: 2007-06 Impact factor: 6.725

Nuclear magnetic resonance studies of the denaturation of ubiquitin.

1. The role of a beta-bulge in the folding of the beta-hairpin structure in ubiquitin.

Review 2. Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes.

3. Observation of protein folding/unfolding dynamics of ubiquitin trapped in agarose gel by single-molecule FRET.

4. Motional properties of unfolded ubiquitin: a model for a random coil protein.

5. Conformation types of ubiquitin [M+8H]8+ Ions from water:methanol solutions: evidence for the N and A States in aqueous solution.

6. Molecular dynamics simulations of the native and partially folded states of ubiquitin: influence of methanol cosolvent, pH, and temperature on the protein structure and dynamics.

7. Solution dependence of the collisional activation of ubiquitin [M + 7H](7+) ions.

8. The regulatory particle of the Saccharomyces cerevisiae proteasome.

9. Molecular dynamics simulations of hydrophobic collapse of ubiquitin.

10. Libraries of random-sequence polypeptides produced with high yield as carboxy-terminal fusions with ubiquitin.