NMR Structural Characterization of Protein Folding Pathways and Intermediates

2000 ◽  
Vol 28 (5) ◽  
pp. A136-A136
Author(s):  
P. E. Wright ◽  
H. J. Dyson
2015 ◽  
Vol 142 (8) ◽  
pp. 085101 ◽  
Author(s):  
Sang Beom Kim ◽  
Carmeline J. Dsilva ◽  
Ioannis G. Kevrekidis ◽  
Pablo G. Debenedetti

Molecules ◽  
2020 ◽  
Vol 25 (23) ◽  
pp. 5551
Author(s):  
Cécile Dubois ◽  
Isaline Herrada ◽  
Philippe Barthe ◽  
Christian Roumestand

High-hydrostatic pressure is an alternative perturbation method that can be used to destabilize globular proteins. Generally perfectly reversible, pressure exerts local effects on regions or domains of a protein containing internal voids, contrary to heat or chemical denaturant that destabilize protein structures uniformly. When combined with NMR spectroscopy, high pressure (HP) allows one to monitor at a residue-level resolution the structural transitions occurring upon unfolding and to determine the kinetic properties of the process. The use of HP-NMR has long been hampered by technical difficulties. Owing to the recent development of commercially available high-pressure sample cells, HP-NMR experiments can now be routinely performed. This review summarizes recent advances of HP-NMR techniques for the characterization at a quasi-atomic resolution of the protein folding energy landscape.


2017 ◽  
Vol 147 (6) ◽  
pp. 064108 ◽  
Author(s):  
S. Orioli ◽  
S. a Beccara ◽  
P. Faccioli

1997 ◽  
Vol 8 (4) ◽  
pp. 400-410 ◽  
Author(s):  
Anthony R Clarke ◽  
Jonathan P Waltho

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