Chaperone Action at the Single-Molecule Level

Chem. Rev., 2014, DOI: 10.1021/cr400326k, 114 (1), pp 660–667 published on 03.09.2014
Chem. Rev., online article
INTRODUCTION: Natively folded proteins generally have a significant number of hydrophobic residues that cluster together to form a hydrophobic core. However, during the vectorial synthesis on the ribosome and subsequent folding, these hydrophobic residues are exposed. Because folding occurs in a highly crowded environment, exposed residues can lead to undesired interactions that irreversibly harm the folding process. In particular, they can result in the formation of misfolded states and aggregation.

TU München
Helmholtz München
MPI of Neurobiology
MPI of Biochemistry