Blobel, Jascha and Schmidl, Sabine and Vidal, David and Nisius, Lydia and Bernado, Pau and Millet, Oscar and Brunner, Eike and Pons, Miquel (2007) Protein tyrosine phosphatase oligomerization studied by a combination of N-15 NMR relaxation and Xe-129 NMR. Effect of buffer containing arginine and glutamic acid. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 129 (18). pp. 5946-5953. ISSN 0002-7863,
Full text not available from this repository. (Request a copy)Abstract
N-15 NMR relaxation and Xe-129 NMR chemical shift measurements offer complementary information to study weak protein-protein interactions. They have been applied to study the oligomerization equilibrium of a low-molecular-weight protein tyrosine phosphatase in the presence of 50 mM arginine and 50 mM glutamic acid. These experimental conditions are shown to enhance specific protein-protein interactions while decreasing nonspecific aggregation. In addition, Xe-129 NMR chemical shifts become selective reporters of one particular oligomer in the presence of arginine and glutamic acid, indicating that a specific Xe binding site is created in the oligomerization process. It is suggested that the multiple effects of arginine and glutamic acid are related to their effective excluded volume that favors specific protein association and the destabilization of partially unfolded forms that preferentially interact with xenon and are responsible for nonspecific protein aggregation.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | HYDRODYNAMIC CALCULATIONS; CONFORMATIONAL-CHANGE; NEGATIVE REGULATION; GLOBULAR-PROTEINS; CHEMICAL-SHIFT; BOVINE HEART; XENON; SPECTROSCOPY; BINDING; DYNAMICS; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Alumni or Retired > Prof. Dr. Eike Brunner |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 10 Dec 2020 09:54 |
| Last Modified: | 10 Dec 2020 09:54 |
| URI: | https://pred.uni-regensburg.de/id/eprint/32769 |
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