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231225s2017 xx |||||o 00| ||eng c |
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|a 10.1016/j.pnmrs.2017.05.003
|2 doi
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|a eng
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|a Roche, Julien
|e verfasserin
|4 aut
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|a Monitoring protein folding through high pressure NMR spectroscopy
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|c 2017
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 11.09.2018
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|a Date Revised 11.09.2018
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2017 Elsevier B.V. All rights reserved.
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|a 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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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Review
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|a Proteins
|2 NLM
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|a Royer, Catherine A
|e verfasserin
|4 aut
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|a Roumestand, Christian
|e verfasserin
|4 aut
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|i Enthalten in
|t Progress in nuclear magnetic resonance spectroscopy
|d 1998
|g 102-103(2017) vom: 15. Nov., Seite 15-31
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|x 1873-3301
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|g volume:102-103
|g year:2017
|g day:15
|g month:11
|g pages:15-31
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|u http://dx.doi.org/10.1016/j.pnmrs.2017.05.003
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