Continuous wave multiquantum electron paramagnetic resonance spectroscopy. III. Theory of intermodulation sidebands

1993 ◽  
Vol 98 (3) ◽  
pp. 1786-1796 ◽  
Author(s):  
Hassane S. Mchaourab ◽  
James S. Hyde
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Continuous Wave ◽  
Electron Paramagnetic Resonance Spectroscopy ◽  
Resonance Spectroscopy ◽  
Paramagnetic Resonance ◽  
Electron Paramagnetic

scholarly journals Protein Conformational Dynamics upon Association with the Surfaces of Lipid Membranes and Engineered Nanoparticles: Insights from Electron Paramagnetic Resonance Spectroscopy

Molecules ◽  
2020 ◽  
Vol 25 (22) ◽  
pp. 5393
Author(s):  
Elka R. Georgieva
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Continuous Wave ◽  
Electron Paramagnetic Resonance Spectroscopy ◽  
Conformational Dynamics ◽  
Engineered Nanoparticles ◽  
Resonance Spectroscopy ◽  
Functional Protein ◽  
Paramagnetic Resonance ◽  
Conformational Rearrangements ◽  
Electron Paramagnetic

Detailed study of conformational rearrangements and dynamics of proteins is central to our understanding of their physiological functions and the loss of function. This review outlines the applications of the electron paramagnetic resonance (EPR) technique to study the structural aspects of proteins transitioning from a solution environment to the states in which they are associated with the surfaces of biological membranes or engineered nanoobjects. In the former case these structural transitions generally underlie functional protein states. The latter case is mostly relevant to the application of protein immobilization in biotechnological industries, developing methods for protein purification, etc. Therefore, evaluating the stability of the protein functional state is particularly important. EPR spectroscopy in the form of continuous-wave EPR or pulse EPR distance measurements in conjunction with protein spin labeling provides highly versatile and sensitive tools to characterize the changes in protein local dynamics as well as large conformational rearrangements. The technique can be widely utilized in studies of both protein-membrane and engineered nanoobject-protein complexes.

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