Structural Studies of Membrane Proteins using Pulsed EPR Spectroscopy

Structural Studies of the Hsp90-Cdc37 Complex Using EPR Spectroscopy

Hsp90 is a molecular chaperone, a vital protein that facilitates the folding and unfolding of a variety of proteins or ‘clients’. Kinases are one such client, with over half of the human kinome dependent on Hsp90 for activation (1). As its name suggests, Hsp90 is a heat shock protein and thus is highly expressed when the cell is under stress to ensure that proteins are folded and active. Its ex...

The Synergetic Effects of Combining Structural Biology and EPR Spectroscopy on Membrane Proteins

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 ...

Pulsed 180-GHz EPR/ENDOR/PELDOR spectroscopy.

Within this review, we describe a home-built pulsed electron paramagnetic resonance (EPR) spectrometer operating at 180 GHz as well as the incorporation of two double resonance techniques, electron nuclear double resonance (ENDOR) and pulsed electron double resonance (PELDOR), along with first applications. Hahn-echo decays on a TEMPO/polystyrene sample are presented, demonstrating that the obs...

Structural studies of membrane proteins using transmission electron microscopy

NMR and EPR studies of membrane transporters.

In order to fulfill their function, membrane transport proteins have to cycle through a number of conformational and/or energetic states. Thus, understanding the role of conformational dynamics seems to be the key for elucidation of the functional mechanism of these proteins. However, membrane proteins in general are often difficult to express heterologously and in sufficient amounts for struct...