S. G. D. Rudiger

This paper describes a method to produce and purify human Tau protein recombinantly in E. coli, yielding stable and pure preparations suitable for in vitro studies.

This study shows that Tau fibrils use π-stacking by arginine side chains to alter protein interactions, attracting specific proteins linked to Alzheimer's and that Hsp90 can suppress these interactions.

The paper shows that MAP7 family proteins activate kinesin-1 by enhancing its microtubule binding and processivity through transient interactions.

This paper proposes a mechanism where Hsp70 and Hsp90 chaperones facilitate protein folding by creating a hydrophobicity gradient, allowing productive folding to occur.

This paper optimizes the production and purification of recombinant human Hsp90β in E. coli to yield a stable, pure, and well-folded protein.