Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB.

Abstract

Hydrogen-deuterium exchange of 39 amide protons of Bacillus amyloliquefaciens ribonuclease (barnase) was analyzed by two-dimensional nuclear magnetic resonance in the presence of micromolar concentrations of the molecular chaperones GroEL and SecB. Both chaperones bound to native barnase under physiological conditions and catalyzed exchange of deeply buried amide protons with solvent. Such exchange required complete unfolding of barnase, which occurred in the complex with the chaperones. Subsequent collapse of unfolded barnase to the exchange-protected folding intermediate was markedly slowed in the presence of GroEL or SecB. Thus, both chaperones have the potential to correct misfolding in proteins by annealing.

Showing 1-10 of 17 extracted citations

Statistics

050100'98'00'02'04'06'08'10'12'14'16
Citations per Year

170 Citations

Semantic Scholar estimates that this publication has received between 40 and 474 citations based on the available data.

See our FAQ for additional information.