Abstract
Protein structures as provided by structural biology such as X-ray crystallography, cryo-electron microscopy and NMR spectroscopy are key elements to understand the function of a protein on the molecular level. Nonetheless, they might be error-prone due to crystallization artifacts or, in particular in case of membrane-imbedded proteins, a mostly artificial environment. In this review, we will introduce different EPR spectroscopy methods as powerful tools to complement and validate structural data gaining insights in the dynamics of proteins and protein complexes such that functional cycles can be derived. We will highlight the use of EPR spectroscopy on membrane-embedded proteins and protein complexes ranging from receptors to secondary active transporters as structural information is still limited in this field and the lipid environment is a particular challenge.
Highlights
Structural biology aims for studying molecular structures and dynamics of biological macromolecules, in particular proteins and nucleic acids, to gain a deeper comprehension of how alterations in their structures affect their function
More frequently information on rare conformations and protein dynamics is gained by nuclear magnetic resonance (NMR) spectroscopy, Förster resonance energy transfer (FRET)
This review summarizes the versatile aspects of electron paramagnetic resonance (EPR) spectroscopy and the synergistic effects resulting from the combination of EPR spectroscopy and structural biology
Summary
Structural biology aims for studying molecular structures and dynamics of biological macromolecules, in particular proteins and nucleic acids, to gain a deeper comprehension of how alterations in their structures affect their function. Mostly X-ray crystallography and cryo-electron microscopy provide structural information of the protein of interest at atomic resolution for a broad molecular weight range [1,2,3]. Based on those structures, complex interfaces can be analyzed, structure-based drugs designed and various mechanisms predicted. Its inherent strength is substantiated in its various applications to proteins, notably to membrane proteins solubilized in detergent or embedded in the lipid bilayer and protein complexes in native-like conditions This technique is not limited by the size or the complexity of the investigated system (for further reviews see e.g., [4,5,6]). This paper highlights the latest progress with special emphasis on applications to different classes of membrane proteins
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