Friday, 09 April, 2010

The many guises of a chaperone

How molecular chaperones influence protein structures

 

Without a class of proteins known as chaperones, life on Earth would not be possible. Chaperones enable newly synthesized proteins to adopt the precise three-dimensional conformation that is necessary for their biological function. Little is known about the changes in molecular structure of chaperones as they help substrate proteins to fold. Now, in collaborative work, research teams of Dr. Dejana Mokranjac and Professor Don C. Lamb of Ludwig-Maximilians-Universität (LMU) in Munich have been able to follow in real time the structural changes that occur in an important type of chaperone as it coaxes an unfolded substrate protein into shape. They discovered that the Ssc1, a member of the so-called HSP70 family of chaperones, can take on a surprising variety of conformations. (Molecular Cell, 9 April 2010).

Press information LMU (english)

Presseinformation der LMU (deutsch)

Publication "The Conformational Dynamics of the Mitochondrial Hsp70 Chaperone"