Slow and bimolecular folding of a de novo designed monomeric protein DS119.

Abstract excerpt

De novo protein design offers a unique means to test and advance our understanding of how proteins fold. However, most current design methods are native structure eccentric and folding kinetics has rarely been considered in the design process. Here, we show that a de novo designed mini-protein DS119, which folds into a βαβ structure, exhibits unusually slow and concentration-dependent folding kinetics. For...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Hydrogen-Ion Concentration
• Share to Kinetics
• Share to Protein Engineering