Monitoring protein folding through high pressure NMR spectroscopy
Copyright © 2017 Elsevier B.V. All rights reserved.
| Veröffentlicht in: | Progress in nuclear magnetic resonance spectroscopy. - 1998. - 102-103(2017) vom: 15. Nov., Seite 15-31 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2017
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| Zugriff auf das übergeordnete Werk: | Progress in nuclear magnetic resonance spectroscopy |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Review Proteins |
| Zusammenfassung: | Copyright © 2017 Elsevier B.V. All rights reserved. High-pressure is a well-known perturbation method used to destabilize globular proteins. It is perfectly reversible, which is essential for a proper thermodynamic characterization of a protein equilibrium. In contrast to other perturbation methods such as heat or chemical denaturant that destabilize protein structures uniformly, pressure exerts local effects on regions or domains of a protein containing internal cavities. When combined with NMR spectroscopy, hydrostatic pressure offers the possibility to monitor at a residue level the structural transitions occurring upon unfolding and to determine the kinetic properties of the process. High-pressure NMR experiments can now be routinely performed, owing to the recent development of commercially available high-pressure sample cells. This review summarizes recent advances and some future directions of high-pressure NMR techniques for the characterization at atomic resolution of the energy landscape of protein folding |
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| Beschreibung: | Date Completed 11.09.2018 Date Revised 11.09.2018 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-3301 |
| DOI: | 10.1016/j.pnmrs.2017.05.003 |