Ernst Lab discover new way to crystallize membrane proteins

7 February 2017|

The laboratory of Dr. Oliver Ernst has used X-ray crystallography to determine the structure of a membrane protein that never left a lipid-bilayer environment (i.e., without the use of conventional detergents). The work, published in Structure and highlighted on the Journal’s cover, was led by postdoctoral fellow Dr. Jana Broecker. Polymer-bounded lipid nanodiscs were used to extract and purify membrane proteins with their surrounding lipids and allowed […]

An image of bacterial chaperone.The molecular chaperone RavA forms amyloids at low pH and elevated temperatures.

When molecular chaperones misbehave

5 July 2016|

Walid Houry’s group together with Simon Sharpe’s group and others at the University of Toronto unexpectedly discovered that a bacterial chaperone forms amyloids under physiologically-relevant acidic conditions at elevated temperatures. The work has been accepted in Structure. Experimental and theoretical studies revealed that the folded core of one of the domains of the chaperones is amyloidogenic and is protected by its N-terminal loop. While molecular chaperones are […]