High-pressure NMR techniques for the study of protein dynamics, folding and aggregation
| Autor: | Julien Roche, Luan M. Nguyen |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Protein Folding Nuclear and High Energy Physics Protein Conformation Globular protein Hydrostatic pressure Biophysics Phi value analysis Protein aggregation 010402 general chemistry 01 natural sciences Biochemistry 03 medical and health sciences Protein structure Hydrostatic Pressure Nuclear Magnetic Resonance Biomolecular chemistry.chemical_classification Quantitative Biology::Biomolecules Protein dynamics Proteins Nuclear magnetic resonance spectroscopy Condensed Matter Physics 0104 chemical sciences Kinetics 030104 developmental biology chemistry Chemical physics Thermodynamics Physical chemistry Protein folding |
| Zdroj: | Journal of Magnetic Resonance. 277:179-185 |
| ISSN: | 1090-7807 |
| DOI: | 10.1016/j.jmr.2017.01.009 |
| Popis: | High-pressure is a well-known perturbation method used to destabilize globular proteins and dissociate protein complexes or aggregates. The heterogeneity of the response to pressure offers a unique opportunity to dissect the thermodynamic contributions to protein stability. In addition, pressure perturbation is generally reversible, which is essential for a proper thermodynamic characterization of a protein equilibrium. When combined with NMR spectroscopy, hydrostatic pressure offers the possibility of monitoring at an atomic resolution the structural transitions occurring upon unfolding and determining the kinetic properties of the process. The recent development of commercially available high-pressure sample cells greatly increased the potential applications for high-pressure NMR experiments that can now be routinely performed. This review summarizes the recent applications and future directions of high-pressure NMR techniques for the characterization of protein conformational fluctuations, protein folding and the stability of protein complexes and aggregates. |
| Databáze: | OpenAIRE |
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