scholarly journals Protein dynamics from nuclear magnetic relaxation

2016 ◽  
Vol 45 (9) ◽  
pp. 2410-2422 ◽  
Author(s):  
Cyril Charlier ◽  
Samuel F. Cousin ◽  
Fabien Ferrage

Protein dynamics are explored by a variety of methods designed to measure nuclear magnetic relaxation rates.

1979 ◽  
Vol 34 (8) ◽  
pp. 944-949 ◽  
Author(s):  
Manfred Holz ◽  
Siegfried Günther ◽  
Otto Lutz ◽  
Alfons Nolle ◽  
Paul-Gerhard Schrade

AbstractLongitudinal nuclear magnetic relaxation rates of 25Mg2+ have been measured in aqueous solutions of MgCl2 and Mg(NO3)2 as a function of concentration. The value of 1/T1, extrapolated for infinite dilution has been compared with the "electrostatic theory" of Hertz. It turned out that the relaxation rate reflects the high cubic symmetry of the first hydration sphere of 25Mg2+ . Using the 1H and 25Mg2+ relaxation rates at finite salt concentration the "ion-ion contributions" to the 25Mg2+ relaxation rates have been determined. They are compared with those in aqueous LiCl solutions. A big change in the 25Mg2+ relaxation rate in MgCl2 solution was found when a little amount of sodium citrate was added.


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