Detection of interaction between protein trytophan residues and small or macromolecular ligands by synchrotron radiation magnetic circular dichroism

2015 ◽  
Vol 7 (5) ◽  
pp. 1667-1671 ◽  
Author(s):  
Ashley J. Hughes ◽  
Timothy R. Rudd ◽  
Gareth S. A. Wright ◽  
David G. Fernig ◽  
Giuliano Siligardi ◽  
...  

Magnetic circular dichroism selectively detects interactions between macromolecules in solution that involve tryptophan–ligand interactions, through changes at 286 nm, and also between proteins and small molecules, such as 5-fluorouridine and superoxide dismutase.

2018 ◽  
Vol 25 (6) ◽  
pp. 1727-1735 ◽  
Author(s):  
J.-P. Kappler ◽  
E. Otero ◽  
W. Li ◽  
L. Joly ◽  
G. Schmerber ◽  
...  

A new ultralow-temperature setup dedicated to soft X-ray absorption spectroscopy and X-ray magnetic circular dichroism (XMCD) experiments is described. Two experiments, performed on the DEIMOS beamline (SOLEIL synchrotron), demonstrate the outstanding performance of this new platform in terms of the lowest achievable temperature under X-ray irradiation (T = 220 mK), the precision in controlling the temperature during measurements as well as the speed of the cooling-down and warming-up procedures. Moreover, owing to the new design of the setup, the eddy-current power is strongly reduced, allowing fast scanning of the magnetic field in XMCD experiments; these performances lead to a powerful device for X-ray spectroscopies on synchrotron-radiation beamlines facilities.


Sign in / Sign up

Export Citation Format

Share Document