Gymnastics of molecular chaperones

Matthias P Mayer

doi:10.1016/j.molcel.2010.07.012

Gymnastics of molecular chaperones

Mol Cell. 2010 Aug 13;39(3):321-31. doi: 10.1016/j.molcel.2010.07.012.

Author

Matthias P Mayer¹

Affiliation

¹ Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH-Allianz, Heidelberg, Germany. m.mayer@zmbh.uni-heidelberg.de

PMID: 20705236
DOI: 10.1016/j.molcel.2010.07.012

Abstract

Molecular chaperones assist folding processes and conformational changes in many proteins. In order to do so, they progress through complex conformational cycles themselves. In this review, I discuss the diverse conformational dynamics of the ATP-dependent chaperones of the Hsp60, Hsp70, Hsp90, and Hsp100 families.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Adenosine Triphosphate / genetics
Adenosine Triphosphate / metabolism*
Animals
Heat-Shock Proteins / genetics
Heat-Shock Proteins / metabolism*
Humans
Protein Conformation

Substances

Heat-Shock Proteins
Adenosine Triphosphate